Charge regulation phenomenon predicted from the modeling of polypeptide electrophoretic mobilities as a relevant mechanism of amyloid‐beta peptide oligomerization

Electrophoretic mobilities of amyloid‐beta (1‐40) and (1‐42) peptides and their aggregates are modeled to study the amyloidogenic pathway associated with Alzheimer´s Disease. The near molecule pH generated by the intraparticle charge regulation phenomenon during the oligomerization of amyloid‐beta (...
Ausführliche Beschreibung

Gespeichert in:

Autor*in:	Deiber, Julio A [verfasserIn] Peirotti, Marta B Piaggio, Maria V

Format:	Artikel
Sprache:	Englisch

Erschienen:	2016

Rechteinformationen:	Nutzungsrecht: © 2016 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim © 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

Schlagwörter:	Amyloid‐beta peptides Peptide oligomerization Charge regulation phenomenon Electrophoretic mobility Amyloid cascade hypothesis

Übergeordnetes Werk:	Enthalten in: Electrophoresis - Weinheim : Wiley-VCH, 1980, 37(2016), 5-6, Seite 711-718
Übergeordnetes Werk:	volume:37 ; year:2016 ; number:5-6 ; pages:711-718

Links:	Volltext Link aufrufen Link aufrufen

DOI / URN:	10.1002/elps.201500391

Katalog-ID:	OLC1973234963

Internformat


LEADER	01000caa a2200265 4500
001	OLC1973234963
003	DE-627
005	20220222021112.0
007	tu
008	160427s2016 xx \|\|\|\|\| 00\| \|\|eng c
024	7		\|a 10.1002/elps.201500391 \|2 doi
028	5	2	\|a PQ20160430
035			\|a (DE-627)OLC1973234963
035			\|a (DE-599)GBVOLC1973234963
035			\|a (PRQ)c1076-e19241162dbe01bdcb9a7888929d35c3c30e7f3fb7186c86da8133736290df1b3
035			\|a (KEY)0204026320160000037000500711chargeregulationphenomenonpredictedfromthemodeling
040			\|a DE-627 \|b ger \|c DE-627 \|e rakwb
041			\|a eng
082	0	4	\|a 540 \|a 570 \|q DNB
082	0	4	\|a 570 \|q AVZ
084			\|a BIODIV \|2 fid
084			\|a 35.29 \|2 bkl
100	1		\|a Deiber, Julio A \|e verfasserin \|4 aut
245	1	0	\|a Charge regulation phenomenon predicted from the modeling of polypeptide electrophoretic mobilities as a relevant mechanism of amyloid‐beta peptide oligomerization
264		1	\|c 2016
336			\|a Text \|b txt \|2 rdacontent
337			\|a ohne Hilfsmittel zu benutzen \|b n \|2 rdamedia
338			\|a Band \|b nc \|2 rdacarrier
520			\|a Electrophoretic mobilities of amyloid‐beta (1‐40) and (1‐42) peptides and their aggregates are modeled to study the amyloidogenic pathway associated with Alzheimer´s Disease. The near molecule pH generated by the intraparticle charge regulation phenomenon during the oligomerization of amyloid‐beta (1‐40) and (1‐42) peptides is evaluated and discussed as a relevant mechanism supporting the “amyloid cascade hypothesis” proposed in the literature. A theoretical framework associated with the oligomerization of amyloid‐beta peptides including simple scaling laws and the consideration of electrokinetic and hydrodynamic global properties of oligomers is presented. The central finding is the explanation of the near molecule pH change toward the pI when the oligomerization number increases. These results allow one to rationalize consecutive physical stages that validate the amyloid cascade hypothesis. Concluding remarks involving mainly the effects of pair and intraparticle charge regulation phenomena on the amyloidogenic pathway with some suggestions for future research are provided.
540			\|a Nutzungsrecht: © 2016 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim
540			\|a © 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
650		4	\|a Amyloid‐beta peptides
650		4	\|a Peptide oligomerization
650		4	\|a Charge regulation phenomenon
650		4	\|a Electrophoretic mobility
650		4	\|a Amyloid cascade hypothesis
700	1		\|a Peirotti, Marta B \|4 oth
700	1		\|a Piaggio, Maria V \|4 oth
773	0	8	\|i Enthalten in \|t Electrophoresis \|d Weinheim : Wiley-VCH, 1980 \|g 37(2016), 5-6, Seite 711-718 \|w (DE-627)130409952 \|w (DE-600)619001-7 \|w (DE-576)015913732 \|x 0173-0835 \|7 nnns
773	1	8	\|g volume:37 \|g year:2016 \|g number:5-6 \|g pages:711-718
856	4	1	\|u http://dx.doi.org/10.1002/elps.201500391 \|3 Volltext
856	4	2	\|u http://onlinelibrary.wiley.com/doi/10.1002/elps.201500391/abstract
856	4	2	\|u http://www.ncbi.nlm.nih.gov/pubmed/26718015
912			\|a GBV_USEFLAG_A
912			\|a SYSFLAG_A
912			\|a GBV_OLC
912			\|a FID-BIODIV
912			\|a SSG-OLC-TEC
912			\|a SSG-OLC-CHE
912			\|a GBV_ILN_70
912			\|a GBV_ILN_267
912			\|a GBV_ILN_2018
912			\|a GBV_ILN_2219
912			\|a GBV_ILN_4012
936	b	k	\|a 35.29 \|q AVZ
951			\|a AR
952			\|d 37 \|j 2016 \|e 5-6 \|h 711-718

Indexfelder

author_variant	j a d ja jad
matchkey_str	article:01730835:2016----::hreeuainhnmnnrdcefoteoeigfoyetdeetohrtcoiiissrlvnmca
hierarchy_sort_str	2016
bklnumber	35.29
publishDate	2016
allfields	10.1002/elps.201500391 doi PQ20160430 (DE-627)OLC1973234963 (DE-599)GBVOLC1973234963 (PRQ)c1076-e19241162dbe01bdcb9a7888929d35c3c30e7f3fb7186c86da8133736290df1b3 (KEY)0204026320160000037000500711chargeregulationphenomenonpredictedfromthemodeling DE-627 ger DE-627 rakwb eng 540 570 DNB 570 AVZ BIODIV fid 35.29 bkl Deiber, Julio A verfasserin aut Charge regulation phenomenon predicted from the modeling of polypeptide electrophoretic mobilities as a relevant mechanism of amyloid‐beta peptide oligomerization 2016 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Electrophoretic mobilities of amyloid‐beta (1‐40) and (1‐42) peptides and their aggregates are modeled to study the amyloidogenic pathway associated with Alzheimer´s Disease. The near molecule pH generated by the intraparticle charge regulation phenomenon during the oligomerization of amyloid‐beta (1‐40) and (1‐42) peptides is evaluated and discussed as a relevant mechanism supporting the “amyloid cascade hypothesis” proposed in the literature. A theoretical framework associated with the oligomerization of amyloid‐beta peptides including simple scaling laws and the consideration of electrokinetic and hydrodynamic global properties of oligomers is presented. The central finding is the explanation of the near molecule pH change toward the pI when the oligomerization number increases. These results allow one to rationalize consecutive physical stages that validate the amyloid cascade hypothesis. Concluding remarks involving mainly the effects of pair and intraparticle charge regulation phenomena on the amyloidogenic pathway with some suggestions for future research are provided. Nutzungsrecht: © 2016 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim © 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim. Amyloid‐beta peptides Peptide oligomerization Charge regulation phenomenon Electrophoretic mobility Amyloid cascade hypothesis Peirotti, Marta B oth Piaggio, Maria V oth Enthalten in Electrophoresis Weinheim : Wiley-VCH, 1980 37(2016), 5-6, Seite 711-718 (DE-627)130409952 (DE-600)619001-7 (DE-576)015913732 0173-0835 nnns volume:37 year:2016 number:5-6 pages:711-718 http://dx.doi.org/10.1002/elps.201500391 Volltext http://onlinelibrary.wiley.com/doi/10.1002/elps.201500391/abstract http://www.ncbi.nlm.nih.gov/pubmed/26718015 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_70 GBV_ILN_267 GBV_ILN_2018 GBV_ILN_2219 GBV_ILN_4012 35.29 AVZ AR 37 2016 5-6 711-718
spelling	10.1002/elps.201500391 doi PQ20160430 (DE-627)OLC1973234963 (DE-599)GBVOLC1973234963 (PRQ)c1076-e19241162dbe01bdcb9a7888929d35c3c30e7f3fb7186c86da8133736290df1b3 (KEY)0204026320160000037000500711chargeregulationphenomenonpredictedfromthemodeling DE-627 ger DE-627 rakwb eng 540 570 DNB 570 AVZ BIODIV fid 35.29 bkl Deiber, Julio A verfasserin aut Charge regulation phenomenon predicted from the modeling of polypeptide electrophoretic mobilities as a relevant mechanism of amyloid‐beta peptide oligomerization 2016 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Electrophoretic mobilities of amyloid‐beta (1‐40) and (1‐42) peptides and their aggregates are modeled to study the amyloidogenic pathway associated with Alzheimer´s Disease. The near molecule pH generated by the intraparticle charge regulation phenomenon during the oligomerization of amyloid‐beta (1‐40) and (1‐42) peptides is evaluated and discussed as a relevant mechanism supporting the “amyloid cascade hypothesis” proposed in the literature. A theoretical framework associated with the oligomerization of amyloid‐beta peptides including simple scaling laws and the consideration of electrokinetic and hydrodynamic global properties of oligomers is presented. The central finding is the explanation of the near molecule pH change toward the pI when the oligomerization number increases. These results allow one to rationalize consecutive physical stages that validate the amyloid cascade hypothesis. Concluding remarks involving mainly the effects of pair and intraparticle charge regulation phenomena on the amyloidogenic pathway with some suggestions for future research are provided. Nutzungsrecht: © 2016 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim © 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim. Amyloid‐beta peptides Peptide oligomerization Charge regulation phenomenon Electrophoretic mobility Amyloid cascade hypothesis Peirotti, Marta B oth Piaggio, Maria V oth Enthalten in Electrophoresis Weinheim : Wiley-VCH, 1980 37(2016), 5-6, Seite 711-718 (DE-627)130409952 (DE-600)619001-7 (DE-576)015913732 0173-0835 nnns volume:37 year:2016 number:5-6 pages:711-718 http://dx.doi.org/10.1002/elps.201500391 Volltext http://onlinelibrary.wiley.com/doi/10.1002/elps.201500391/abstract http://www.ncbi.nlm.nih.gov/pubmed/26718015 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_70 GBV_ILN_267 GBV_ILN_2018 GBV_ILN_2219 GBV_ILN_4012 35.29 AVZ AR 37 2016 5-6 711-718
allfields_unstemmed	10.1002/elps.201500391 doi PQ20160430 (DE-627)OLC1973234963 (DE-599)GBVOLC1973234963 (PRQ)c1076-e19241162dbe01bdcb9a7888929d35c3c30e7f3fb7186c86da8133736290df1b3 (KEY)0204026320160000037000500711chargeregulationphenomenonpredictedfromthemodeling DE-627 ger DE-627 rakwb eng 540 570 DNB 570 AVZ BIODIV fid 35.29 bkl Deiber, Julio A verfasserin aut Charge regulation phenomenon predicted from the modeling of polypeptide electrophoretic mobilities as a relevant mechanism of amyloid‐beta peptide oligomerization 2016 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Electrophoretic mobilities of amyloid‐beta (1‐40) and (1‐42) peptides and their aggregates are modeled to study the amyloidogenic pathway associated with Alzheimer´s Disease. The near molecule pH generated by the intraparticle charge regulation phenomenon during the oligomerization of amyloid‐beta (1‐40) and (1‐42) peptides is evaluated and discussed as a relevant mechanism supporting the “amyloid cascade hypothesis” proposed in the literature. A theoretical framework associated with the oligomerization of amyloid‐beta peptides including simple scaling laws and the consideration of electrokinetic and hydrodynamic global properties of oligomers is presented. The central finding is the explanation of the near molecule pH change toward the pI when the oligomerization number increases. These results allow one to rationalize consecutive physical stages that validate the amyloid cascade hypothesis. Concluding remarks involving mainly the effects of pair and intraparticle charge regulation phenomena on the amyloidogenic pathway with some suggestions for future research are provided. Nutzungsrecht: © 2016 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim © 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim. Amyloid‐beta peptides Peptide oligomerization Charge regulation phenomenon Electrophoretic mobility Amyloid cascade hypothesis Peirotti, Marta B oth Piaggio, Maria V oth Enthalten in Electrophoresis Weinheim : Wiley-VCH, 1980 37(2016), 5-6, Seite 711-718 (DE-627)130409952 (DE-600)619001-7 (DE-576)015913732 0173-0835 nnns volume:37 year:2016 number:5-6 pages:711-718 http://dx.doi.org/10.1002/elps.201500391 Volltext http://onlinelibrary.wiley.com/doi/10.1002/elps.201500391/abstract http://www.ncbi.nlm.nih.gov/pubmed/26718015 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_70 GBV_ILN_267 GBV_ILN_2018 GBV_ILN_2219 GBV_ILN_4012 35.29 AVZ AR 37 2016 5-6 711-718
allfieldsGer	10.1002/elps.201500391 doi PQ20160430 (DE-627)OLC1973234963 (DE-599)GBVOLC1973234963 (PRQ)c1076-e19241162dbe01bdcb9a7888929d35c3c30e7f3fb7186c86da8133736290df1b3 (KEY)0204026320160000037000500711chargeregulationphenomenonpredictedfromthemodeling DE-627 ger DE-627 rakwb eng 540 570 DNB 570 AVZ BIODIV fid 35.29 bkl Deiber, Julio A verfasserin aut Charge regulation phenomenon predicted from the modeling of polypeptide electrophoretic mobilities as a relevant mechanism of amyloid‐beta peptide oligomerization 2016 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Electrophoretic mobilities of amyloid‐beta (1‐40) and (1‐42) peptides and their aggregates are modeled to study the amyloidogenic pathway associated with Alzheimer´s Disease. The near molecule pH generated by the intraparticle charge regulation phenomenon during the oligomerization of amyloid‐beta (1‐40) and (1‐42) peptides is evaluated and discussed as a relevant mechanism supporting the “amyloid cascade hypothesis” proposed in the literature. A theoretical framework associated with the oligomerization of amyloid‐beta peptides including simple scaling laws and the consideration of electrokinetic and hydrodynamic global properties of oligomers is presented. The central finding is the explanation of the near molecule pH change toward the pI when the oligomerization number increases. These results allow one to rationalize consecutive physical stages that validate the amyloid cascade hypothesis. Concluding remarks involving mainly the effects of pair and intraparticle charge regulation phenomena on the amyloidogenic pathway with some suggestions for future research are provided. Nutzungsrecht: © 2016 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim © 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim. Amyloid‐beta peptides Peptide oligomerization Charge regulation phenomenon Electrophoretic mobility Amyloid cascade hypothesis Peirotti, Marta B oth Piaggio, Maria V oth Enthalten in Electrophoresis Weinheim : Wiley-VCH, 1980 37(2016), 5-6, Seite 711-718 (DE-627)130409952 (DE-600)619001-7 (DE-576)015913732 0173-0835 nnns volume:37 year:2016 number:5-6 pages:711-718 http://dx.doi.org/10.1002/elps.201500391 Volltext http://onlinelibrary.wiley.com/doi/10.1002/elps.201500391/abstract http://www.ncbi.nlm.nih.gov/pubmed/26718015 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_70 GBV_ILN_267 GBV_ILN_2018 GBV_ILN_2219 GBV_ILN_4012 35.29 AVZ AR 37 2016 5-6 711-718
allfieldsSound	10.1002/elps.201500391 doi PQ20160430 (DE-627)OLC1973234963 (DE-599)GBVOLC1973234963 (PRQ)c1076-e19241162dbe01bdcb9a7888929d35c3c30e7f3fb7186c86da8133736290df1b3 (KEY)0204026320160000037000500711chargeregulationphenomenonpredictedfromthemodeling DE-627 ger DE-627 rakwb eng 540 570 DNB 570 AVZ BIODIV fid 35.29 bkl Deiber, Julio A verfasserin aut Charge regulation phenomenon predicted from the modeling of polypeptide electrophoretic mobilities as a relevant mechanism of amyloid‐beta peptide oligomerization 2016 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Electrophoretic mobilities of amyloid‐beta (1‐40) and (1‐42) peptides and their aggregates are modeled to study the amyloidogenic pathway associated with Alzheimer´s Disease. The near molecule pH generated by the intraparticle charge regulation phenomenon during the oligomerization of amyloid‐beta (1‐40) and (1‐42) peptides is evaluated and discussed as a relevant mechanism supporting the “amyloid cascade hypothesis” proposed in the literature. A theoretical framework associated with the oligomerization of amyloid‐beta peptides including simple scaling laws and the consideration of electrokinetic and hydrodynamic global properties of oligomers is presented. The central finding is the explanation of the near molecule pH change toward the pI when the oligomerization number increases. These results allow one to rationalize consecutive physical stages that validate the amyloid cascade hypothesis. Concluding remarks involving mainly the effects of pair and intraparticle charge regulation phenomena on the amyloidogenic pathway with some suggestions for future research are provided. Nutzungsrecht: © 2016 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim © 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim. Amyloid‐beta peptides Peptide oligomerization Charge regulation phenomenon Electrophoretic mobility Amyloid cascade hypothesis Peirotti, Marta B oth Piaggio, Maria V oth Enthalten in Electrophoresis Weinheim : Wiley-VCH, 1980 37(2016), 5-6, Seite 711-718 (DE-627)130409952 (DE-600)619001-7 (DE-576)015913732 0173-0835 nnns volume:37 year:2016 number:5-6 pages:711-718 http://dx.doi.org/10.1002/elps.201500391 Volltext http://onlinelibrary.wiley.com/doi/10.1002/elps.201500391/abstract http://www.ncbi.nlm.nih.gov/pubmed/26718015 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_70 GBV_ILN_267 GBV_ILN_2018 GBV_ILN_2219 GBV_ILN_4012 35.29 AVZ AR 37 2016 5-6 711-718
language	English
source	Enthalten in Electrophoresis 37(2016), 5-6, Seite 711-718 volume:37 year:2016 number:5-6 pages:711-718
sourceStr	Enthalten in Electrophoresis 37(2016), 5-6, Seite 711-718 volume:37 year:2016 number:5-6 pages:711-718
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	Amyloid‐beta peptides Peptide oligomerization Charge regulation phenomenon Electrophoretic mobility Amyloid cascade hypothesis
dewey-raw	540
isfreeaccess_bool	false
container_title	Electrophoresis
authorswithroles_txt_mv	Deiber, Julio A @@aut@@ Peirotti, Marta B @@oth@@ Piaggio, Maria V @@oth@@
publishDateDaySort_date	2016-01-01T00:00:00Z
hierarchy_top_id	130409952
dewey-sort	3540
id	OLC1973234963
language_de	englisch
fullrecord	<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a2200265 4500</leader><controlfield tag="001">OLC1973234963</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20220222021112.0</controlfield><controlfield tag="007">tu</controlfield><controlfield tag="008">160427s2016 xx \|\|\|\|\| 00\| \|\|eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1002/elps.201500391</subfield><subfield code="2">doi</subfield></datafield><datafield tag="028" ind1="5" ind2="2"><subfield code="a">PQ20160430</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)OLC1973234963</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVOLC1973234963</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(PRQ)c1076-e19241162dbe01bdcb9a7888929d35c3c30e7f3fb7186c86da8133736290df1b3</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(KEY)0204026320160000037000500711chargeregulationphenomenonpredictedfromthemodeling</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="082" ind1="0" ind2="4"><subfield code="a">540</subfield><subfield code="a">570</subfield><subfield code="q">DNB</subfield></datafield><datafield tag="082" ind1="0" ind2="4"><subfield code="a">570</subfield><subfield code="q">AVZ</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">BIODIV</subfield><subfield code="2">fid</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">35.29</subfield><subfield code="2">bkl</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Deiber, Julio A</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Charge regulation phenomenon predicted from the modeling of polypeptide electrophoretic mobilities as a relevant mechanism of amyloid‐beta peptide oligomerization</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2016</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">ohne Hilfsmittel zu benutzen</subfield><subfield code="b">n</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Band</subfield><subfield code="b">nc</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Electrophoretic mobilities of amyloid‐beta (1‐40) and (1‐42) peptides and their aggregates are modeled to study the amyloidogenic pathway associated with Alzheimer´s Disease. The near molecule pH generated by the intraparticle charge regulation phenomenon during the oligomerization of amyloid‐beta (1‐40) and (1‐42) peptides is evaluated and discussed as a relevant mechanism supporting the “amyloid cascade hypothesis” proposed in the literature. A theoretical framework associated with the oligomerization of amyloid‐beta peptides including simple scaling laws and the consideration of electrokinetic and hydrodynamic global properties of oligomers is presented. The central finding is the explanation of the near molecule pH change toward the pI when the oligomerization number increases. These results allow one to rationalize consecutive physical stages that validate the amyloid cascade hypothesis. Concluding remarks involving mainly the effects of pair and intraparticle charge regulation phenomena on the amyloidogenic pathway with some suggestions for future research are provided.</subfield></datafield><datafield tag="540" ind1=" " ind2=" "><subfield code="a">Nutzungsrecht: © 2016 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim</subfield></datafield><datafield tag="540" ind1=" " ind2=" "><subfield code="a">© 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Amyloid‐beta peptides</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Peptide oligomerization</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Charge regulation phenomenon</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Electrophoretic mobility</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Amyloid cascade hypothesis</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Peirotti, Marta B</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Piaggio, Maria V</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">Electrophoresis</subfield><subfield code="d">Weinheim : Wiley-VCH, 1980</subfield><subfield code="g">37(2016), 5-6, Seite 711-718</subfield><subfield code="w">(DE-627)130409952</subfield><subfield code="w">(DE-600)619001-7</subfield><subfield code="w">(DE-576)015913732</subfield><subfield code="x">0173-0835</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:37</subfield><subfield code="g">year:2016</subfield><subfield code="g">number:5-6</subfield><subfield code="g">pages:711-718</subfield></datafield><datafield tag="856" ind1="4" ind2="1"><subfield code="u">http://dx.doi.org/10.1002/elps.201500391</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="856" ind1="4" ind2="2"><subfield code="u">http://onlinelibrary.wiley.com/doi/10.1002/elps.201500391/abstract</subfield></datafield><datafield tag="856" ind1="4" ind2="2"><subfield code="u">http://www.ncbi.nlm.nih.gov/pubmed/26718015</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SYSFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_OLC</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">FID-BIODIV</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-TEC</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-CHE</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_70</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_267</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2018</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2219</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4012</subfield></datafield><datafield tag="936" ind1="b" ind2="k"><subfield code="a">35.29</subfield><subfield code="q">AVZ</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">37</subfield><subfield code="j">2016</subfield><subfield code="e">5-6</subfield><subfield code="h">711-718</subfield></datafield></record></collection>
author	Deiber, Julio A
spellingShingle	Deiber, Julio A ddc 540 ddc 570 fid BIODIV bkl 35.29 misc Amyloid‐beta peptides misc Peptide oligomerization misc Charge regulation phenomenon misc Electrophoretic mobility misc Amyloid cascade hypothesis Charge regulation phenomenon predicted from the modeling of polypeptide electrophoretic mobilities as a relevant mechanism of amyloid‐beta peptide oligomerization
authorStr	Deiber, Julio A
ppnlink_with_tag_str_mv	@@773@@(DE-627)130409952
format	Article
dewey-ones	540 - Chemistry & allied sciences 570 - Life sciences; biology
delete_txt_mv	keep
author_role	aut
collection	OLC
remote_str	false
illustrated	Not Illustrated
issn	0173-0835
topic_title	540 570 DNB 570 AVZ BIODIV fid 35.29 bkl Charge regulation phenomenon predicted from the modeling of polypeptide electrophoretic mobilities as a relevant mechanism of amyloid‐beta peptide oligomerization Amyloid‐beta peptides Peptide oligomerization Charge regulation phenomenon Electrophoretic mobility Amyloid cascade hypothesis
topic	ddc 540 ddc 570 fid BIODIV bkl 35.29 misc Amyloid‐beta peptides misc Peptide oligomerization misc Charge regulation phenomenon misc Electrophoretic mobility misc Amyloid cascade hypothesis
topic_unstemmed	ddc 540 ddc 570 fid BIODIV bkl 35.29 misc Amyloid‐beta peptides misc Peptide oligomerization misc Charge regulation phenomenon misc Electrophoretic mobility misc Amyloid cascade hypothesis
topic_browse	ddc 540 ddc 570 fid BIODIV bkl 35.29 misc Amyloid‐beta peptides misc Peptide oligomerization misc Charge regulation phenomenon misc Electrophoretic mobility misc Amyloid cascade hypothesis
format_facet	Aufsätze Gedruckte Aufsätze
format_main_str_mv	Text Zeitschrift/Artikel
carriertype_str_mv	nc
author2_variant	m b p mb mbp m v p mv mvp
hierarchy_parent_title	Electrophoresis
hierarchy_parent_id	130409952
dewey-tens	540 - Chemistry 570 - Life sciences; biology
hierarchy_top_title	Electrophoresis
isfreeaccess_txt	false
familylinks_str_mv	(DE-627)130409952 (DE-600)619001-7 (DE-576)015913732
title	Charge regulation phenomenon predicted from the modeling of polypeptide electrophoretic mobilities as a relevant mechanism of amyloid‐beta peptide oligomerization
ctrlnum	(DE-627)OLC1973234963 (DE-599)GBVOLC1973234963 (PRQ)c1076-e19241162dbe01bdcb9a7888929d35c3c30e7f3fb7186c86da8133736290df1b3 (KEY)0204026320160000037000500711chargeregulationphenomenonpredictedfromthemodeling
title_full	Charge regulation phenomenon predicted from the modeling of polypeptide electrophoretic mobilities as a relevant mechanism of amyloid‐beta peptide oligomerization
author_sort	Deiber, Julio A
journal	Electrophoresis
journalStr	Electrophoresis
lang_code	eng
isOA_bool	false
dewey-hundreds	500 - Science
recordtype	marc
publishDateSort	2016
contenttype_str_mv	txt
container_start_page	711
author_browse	Deiber, Julio A
container_volume	37
class	540 570 DNB 570 AVZ BIODIV fid 35.29 bkl
format_se	Aufsätze
author-letter	Deiber, Julio A
doi_str_mv	10.1002/elps.201500391
dewey-full	540 570
title_sort	charge regulation phenomenon predicted from the modeling of polypeptide electrophoretic mobilities as a relevant mechanism of amyloid‐beta peptide oligomerization
title_auth	Charge regulation phenomenon predicted from the modeling of polypeptide electrophoretic mobilities as a relevant mechanism of amyloid‐beta peptide oligomerization
abstract	Electrophoretic mobilities of amyloid‐beta (1‐40) and (1‐42) peptides and their aggregates are modeled to study the amyloidogenic pathway associated with Alzheimer´s Disease. The near molecule pH generated by the intraparticle charge regulation phenomenon during the oligomerization of amyloid‐beta (1‐40) and (1‐42) peptides is evaluated and discussed as a relevant mechanism supporting the “amyloid cascade hypothesis” proposed in the literature. A theoretical framework associated with the oligomerization of amyloid‐beta peptides including simple scaling laws and the consideration of electrokinetic and hydrodynamic global properties of oligomers is presented. The central finding is the explanation of the near molecule pH change toward the pI when the oligomerization number increases. These results allow one to rationalize consecutive physical stages that validate the amyloid cascade hypothesis. Concluding remarks involving mainly the effects of pair and intraparticle charge regulation phenomena on the amyloidogenic pathway with some suggestions for future research are provided.
abstractGer	Electrophoretic mobilities of amyloid‐beta (1‐40) and (1‐42) peptides and their aggregates are modeled to study the amyloidogenic pathway associated with Alzheimer´s Disease. The near molecule pH generated by the intraparticle charge regulation phenomenon during the oligomerization of amyloid‐beta (1‐40) and (1‐42) peptides is evaluated and discussed as a relevant mechanism supporting the “amyloid cascade hypothesis” proposed in the literature. A theoretical framework associated with the oligomerization of amyloid‐beta peptides including simple scaling laws and the consideration of electrokinetic and hydrodynamic global properties of oligomers is presented. The central finding is the explanation of the near molecule pH change toward the pI when the oligomerization number increases. These results allow one to rationalize consecutive physical stages that validate the amyloid cascade hypothesis. Concluding remarks involving mainly the effects of pair and intraparticle charge regulation phenomena on the amyloidogenic pathway with some suggestions for future research are provided.
abstract_unstemmed	Electrophoretic mobilities of amyloid‐beta (1‐40) and (1‐42) peptides and their aggregates are modeled to study the amyloidogenic pathway associated with Alzheimer´s Disease. The near molecule pH generated by the intraparticle charge regulation phenomenon during the oligomerization of amyloid‐beta (1‐40) and (1‐42) peptides is evaluated and discussed as a relevant mechanism supporting the “amyloid cascade hypothesis” proposed in the literature. A theoretical framework associated with the oligomerization of amyloid‐beta peptides including simple scaling laws and the consideration of electrokinetic and hydrodynamic global properties of oligomers is presented. The central finding is the explanation of the near molecule pH change toward the pI when the oligomerization number increases. These results allow one to rationalize consecutive physical stages that validate the amyloid cascade hypothesis. Concluding remarks involving mainly the effects of pair and intraparticle charge regulation phenomena on the amyloidogenic pathway with some suggestions for future research are provided.
collection_details	GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_70 GBV_ILN_267 GBV_ILN_2018 GBV_ILN_2219 GBV_ILN_4012
container_issue	5-6
title_short	Charge regulation phenomenon predicted from the modeling of polypeptide electrophoretic mobilities as a relevant mechanism of amyloid‐beta peptide oligomerization
url	http://dx.doi.org/10.1002/elps.201500391 http://onlinelibrary.wiley.com/doi/10.1002/elps.201500391/abstract http://www.ncbi.nlm.nih.gov/pubmed/26718015
remote_bool	false
author2	Peirotti, Marta B Piaggio, Maria V
author2Str	Peirotti, Marta B Piaggio, Maria V
ppnlink	130409952
mediatype_str_mv	n
isOA_txt	false
hochschulschrift_bool	false
author2_role	oth oth
doi_str	10.1002/elps.201500391
up_date	2024-07-04T01:58:09.919Z
_version_	1803611841411153920
fullrecord_marcxml	<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a2200265 4500</leader><controlfield tag="001">OLC1973234963</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20220222021112.0</controlfield><controlfield tag="007">tu</controlfield><controlfield tag="008">160427s2016 xx \|\|\|\|\| 00\| \|\|eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1002/elps.201500391</subfield><subfield code="2">doi</subfield></datafield><datafield tag="028" ind1="5" ind2="2"><subfield code="a">PQ20160430</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)OLC1973234963</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVOLC1973234963</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(PRQ)c1076-e19241162dbe01bdcb9a7888929d35c3c30e7f3fb7186c86da8133736290df1b3</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(KEY)0204026320160000037000500711chargeregulationphenomenonpredictedfromthemodeling</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="082" ind1="0" ind2="4"><subfield code="a">540</subfield><subfield code="a">570</subfield><subfield code="q">DNB</subfield></datafield><datafield tag="082" ind1="0" ind2="4"><subfield code="a">570</subfield><subfield code="q">AVZ</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">BIODIV</subfield><subfield code="2">fid</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">35.29</subfield><subfield code="2">bkl</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Deiber, Julio A</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Charge regulation phenomenon predicted from the modeling of polypeptide electrophoretic mobilities as a relevant mechanism of amyloid‐beta peptide oligomerization</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2016</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">ohne Hilfsmittel zu benutzen</subfield><subfield code="b">n</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Band</subfield><subfield code="b">nc</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Electrophoretic mobilities of amyloid‐beta (1‐40) and (1‐42) peptides and their aggregates are modeled to study the amyloidogenic pathway associated with Alzheimer´s Disease. The near molecule pH generated by the intraparticle charge regulation phenomenon during the oligomerization of amyloid‐beta (1‐40) and (1‐42) peptides is evaluated and discussed as a relevant mechanism supporting the “amyloid cascade hypothesis” proposed in the literature. A theoretical framework associated with the oligomerization of amyloid‐beta peptides including simple scaling laws and the consideration of electrokinetic and hydrodynamic global properties of oligomers is presented. The central finding is the explanation of the near molecule pH change toward the pI when the oligomerization number increases. These results allow one to rationalize consecutive physical stages that validate the amyloid cascade hypothesis. Concluding remarks involving mainly the effects of pair and intraparticle charge regulation phenomena on the amyloidogenic pathway with some suggestions for future research are provided.</subfield></datafield><datafield tag="540" ind1=" " ind2=" "><subfield code="a">Nutzungsrecht: © 2016 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim</subfield></datafield><datafield tag="540" ind1=" " ind2=" "><subfield code="a">© 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Amyloid‐beta peptides</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Peptide oligomerization</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Charge regulation phenomenon</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Electrophoretic mobility</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Amyloid cascade hypothesis</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Peirotti, Marta B</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Piaggio, Maria V</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">Electrophoresis</subfield><subfield code="d">Weinheim : Wiley-VCH, 1980</subfield><subfield code="g">37(2016), 5-6, Seite 711-718</subfield><subfield code="w">(DE-627)130409952</subfield><subfield code="w">(DE-600)619001-7</subfield><subfield code="w">(DE-576)015913732</subfield><subfield code="x">0173-0835</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:37</subfield><subfield code="g">year:2016</subfield><subfield code="g">number:5-6</subfield><subfield code="g">pages:711-718</subfield></datafield><datafield tag="856" ind1="4" ind2="1"><subfield code="u">http://dx.doi.org/10.1002/elps.201500391</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="856" ind1="4" ind2="2"><subfield code="u">http://onlinelibrary.wiley.com/doi/10.1002/elps.201500391/abstract</subfield></datafield><datafield tag="856" ind1="4" ind2="2"><subfield code="u">http://www.ncbi.nlm.nih.gov/pubmed/26718015</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SYSFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_OLC</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">FID-BIODIV</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-TEC</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-CHE</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_70</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_267</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2018</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2219</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4012</subfield></datafield><datafield tag="936" ind1="b" ind2="k"><subfield code="a">35.29</subfield><subfield code="q">AVZ</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">37</subfield><subfield code="j">2016</subfield><subfield code="e">5-6</subfield><subfield code="h">711-718</subfield></datafield></record></collection>
score	7.400529

Nicht das Richtige dabei?

Schreiben Sie uns!

Charge regulation phenomenon predicted from the modeling of polypeptide electrophoretic mobilities as a relevant mechanism of amyloid‐beta peptide oligomerization

Nicht das Richtige dabei?

Zugang & Verfügbarkeit

Vorhandene Bände

Nicht das Richtige dabei?