Atomic Force Microscopy Reveals the Mechanobiology of Lytic Peptide Action on Bacteria

Increasing rates of antimicrobial-resistant medically important bacteria require the development of new, effective therapeutics, of which antimicrobial peptides (AMPs) are among the promising candidates. Many AMPs are membrane-active, but their mode of action in killing bacteria or in inhibiting the...
Ausführliche Beschreibung

Gespeichert in:

Autor*in:	Mularski, Anna [verfasserIn] Wilksch, Jonathan J Wang, Huabin Hossain, Mohammed Akhter Wade, John D Separovic, Frances Strugnell, Richard A Gee, Michelle L

Format:	Artikel
Sprache:	Englisch

Erschienen:	2015

Systematik:	VA 5760

Übergeordnetes Werk:	Enthalten in: Langmuir - Washington, DC : ACS Publ., 1985, 31(2015), 22, Seite 6164
Übergeordnetes Werk:	volume:31 ; year:2015 ; number:22 ; pages:6164

Links:	Link aufrufen

Katalog-ID:	OLC1957081163

Internformat


LEADER	01000caa a2200265 4500
001	OLC1957081163
003	DE-627
005	20230515194422.0
007	tu
008	160206s2015 xx \|\|\|\|\| 00\| \|\|eng c
028	5	2	\|a PQ20160617
035			\|a (DE-627)OLC1957081163
035			\|a (DE-599)GBVOLC1957081163
035			\|a (PRQ)p834-cf0d66cce5e091e4d49f73e62927f6cbb9b8a7266b994eb02f47b211774c1f5b0
035			\|a (KEY)0138429520150000031002206164atomicforcemicroscopyrevealsthemechanobiologyoflyt
040			\|a DE-627 \|b ger \|c DE-627 \|e rakwb
041			\|a eng
082	0	4	\|a 670 \|a 540 \|q DE-600
084			\|a VA 5760 \|q AVZ \|2 rvk
084			\|a 35.18 \|2 bkl
100	1		\|a Mularski, Anna \|e verfasserin \|4 aut
245	1	0	\|a Atomic Force Microscopy Reveals the Mechanobiology of Lytic Peptide Action on Bacteria
264		1	\|c 2015
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 Increasing rates of antimicrobial-resistant medically important bacteria require the development of new, effective therapeutics, of which antimicrobial peptides (AMPs) are among the promising candidates. Many AMPs are membrane-active, but their mode of action in killing bacteria or in inhibiting their growth remains elusive. This study used atomic force microscopy (AFM) to probe the mechanobiology of a model AMP (a derivative of melittin) on living Klebsiella pneumoniae bacterial cells. We performed in situ biophysical measurements to understand how the melittin peptide modulates various biophysical behaviors of individual bacteria, including the turgor pressure, cell wall elasticity, and bacterial capsule thickness and organization. Exposure of K. pneumoniae to the peptide had a significant effect on the turgor pressure and Young's modulus of the cell wall. The turgor pressure increased upon peptide addition followed by a later decrease, suggesting that cell lysis occurred and pressure was lost through destruction of the cell envelope. The Young's modulus also increased, indicating that interaction with the peptide increased the rigidity of the cell wall. The bacterial capsule did not prevent cell lysis by the peptide, and surprisingly, the capsule appeared unaffected by exposure to the peptide, as capsule thickness and inferred organization were within the control limits, determined by mechanical measurements. These data show that AFM measurements may provide valuable insights into the physical events that precede bacterial lysis by AMPs.
700	1		\|a Wilksch, Jonathan J \|4 oth
700	1		\|a Wang, Huabin \|4 oth
700	1		\|a Hossain, Mohammed Akhter \|4 oth
700	1		\|a Wade, John D \|4 oth
700	1		\|a Separovic, Frances \|4 oth
700	1		\|a Strugnell, Richard A \|4 oth
700	1		\|a Gee, Michelle L \|4 oth
773	0	8	\|i Enthalten in \|t Langmuir \|d Washington, DC : ACS Publ., 1985 \|g 31(2015), 22, Seite 6164 \|w (DE-627)129170690 \|w (DE-600)50983-8 \|w (DE-576)01445520X \|x 0743-7463 \|7 nnns
773	1	8	\|g volume:31 \|g year:2015 \|g number:22 \|g pages:6164
856	4	2	\|u http://www.ncbi.nlm.nih.gov/pubmed/25978768
912			\|a GBV_USEFLAG_A
912			\|a SYSFLAG_A
912			\|a GBV_OLC
912			\|a SSG-OLC-TEC
912			\|a SSG-OLC-CHE
912			\|a SSG-OLC-PHA
912			\|a SSG-OLC-DE-84
912			\|a GBV_ILN_23
912			\|a GBV_ILN_70
912			\|a GBV_ILN_2006
912			\|a GBV_ILN_2007
936	r	v	\|a VA 5760
936	b	k	\|a 35.18 \|q AVZ
951			\|a AR
952			\|d 31 \|j 2015 \|e 22 \|h 6164

Indexfelder

author_variant	a m am
matchkey_str	article:07437463:2015----::tmcocmcocprvashmcaoilgoltce
hierarchy_sort_str	2015
bklnumber	35.18
publishDate	2015
allfields	PQ20160617 (DE-627)OLC1957081163 (DE-599)GBVOLC1957081163 (PRQ)p834-cf0d66cce5e091e4d49f73e62927f6cbb9b8a7266b994eb02f47b211774c1f5b0 (KEY)0138429520150000031002206164atomicforcemicroscopyrevealsthemechanobiologyoflyt DE-627 ger DE-627 rakwb eng 670 540 DE-600 VA 5760 AVZ rvk 35.18 bkl Mularski, Anna verfasserin aut Atomic Force Microscopy Reveals the Mechanobiology of Lytic Peptide Action on Bacteria 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Increasing rates of antimicrobial-resistant medically important bacteria require the development of new, effective therapeutics, of which antimicrobial peptides (AMPs) are among the promising candidates. Many AMPs are membrane-active, but their mode of action in killing bacteria or in inhibiting their growth remains elusive. This study used atomic force microscopy (AFM) to probe the mechanobiology of a model AMP (a derivative of melittin) on living Klebsiella pneumoniae bacterial cells. We performed in situ biophysical measurements to understand how the melittin peptide modulates various biophysical behaviors of individual bacteria, including the turgor pressure, cell wall elasticity, and bacterial capsule thickness and organization. Exposure of K. pneumoniae to the peptide had a significant effect on the turgor pressure and Young's modulus of the cell wall. The turgor pressure increased upon peptide addition followed by a later decrease, suggesting that cell lysis occurred and pressure was lost through destruction of the cell envelope. The Young's modulus also increased, indicating that interaction with the peptide increased the rigidity of the cell wall. The bacterial capsule did not prevent cell lysis by the peptide, and surprisingly, the capsule appeared unaffected by exposure to the peptide, as capsule thickness and inferred organization were within the control limits, determined by mechanical measurements. These data show that AFM measurements may provide valuable insights into the physical events that precede bacterial lysis by AMPs. Wilksch, Jonathan J oth Wang, Huabin oth Hossain, Mohammed Akhter oth Wade, John D oth Separovic, Frances oth Strugnell, Richard A oth Gee, Michelle L oth Enthalten in Langmuir Washington, DC : ACS Publ., 1985 31(2015), 22, Seite 6164 (DE-627)129170690 (DE-600)50983-8 (DE-576)01445520X 0743-7463 nnns volume:31 year:2015 number:22 pages:6164 http://www.ncbi.nlm.nih.gov/pubmed/25978768 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_23 GBV_ILN_70 GBV_ILN_2006 GBV_ILN_2007 VA 5760 35.18 AVZ AR 31 2015 22 6164
spelling	PQ20160617 (DE-627)OLC1957081163 (DE-599)GBVOLC1957081163 (PRQ)p834-cf0d66cce5e091e4d49f73e62927f6cbb9b8a7266b994eb02f47b211774c1f5b0 (KEY)0138429520150000031002206164atomicforcemicroscopyrevealsthemechanobiologyoflyt DE-627 ger DE-627 rakwb eng 670 540 DE-600 VA 5760 AVZ rvk 35.18 bkl Mularski, Anna verfasserin aut Atomic Force Microscopy Reveals the Mechanobiology of Lytic Peptide Action on Bacteria 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Increasing rates of antimicrobial-resistant medically important bacteria require the development of new, effective therapeutics, of which antimicrobial peptides (AMPs) are among the promising candidates. Many AMPs are membrane-active, but their mode of action in killing bacteria or in inhibiting their growth remains elusive. This study used atomic force microscopy (AFM) to probe the mechanobiology of a model AMP (a derivative of melittin) on living Klebsiella pneumoniae bacterial cells. We performed in situ biophysical measurements to understand how the melittin peptide modulates various biophysical behaviors of individual bacteria, including the turgor pressure, cell wall elasticity, and bacterial capsule thickness and organization. Exposure of K. pneumoniae to the peptide had a significant effect on the turgor pressure and Young's modulus of the cell wall. The turgor pressure increased upon peptide addition followed by a later decrease, suggesting that cell lysis occurred and pressure was lost through destruction of the cell envelope. The Young's modulus also increased, indicating that interaction with the peptide increased the rigidity of the cell wall. The bacterial capsule did not prevent cell lysis by the peptide, and surprisingly, the capsule appeared unaffected by exposure to the peptide, as capsule thickness and inferred organization were within the control limits, determined by mechanical measurements. These data show that AFM measurements may provide valuable insights into the physical events that precede bacterial lysis by AMPs. Wilksch, Jonathan J oth Wang, Huabin oth Hossain, Mohammed Akhter oth Wade, John D oth Separovic, Frances oth Strugnell, Richard A oth Gee, Michelle L oth Enthalten in Langmuir Washington, DC : ACS Publ., 1985 31(2015), 22, Seite 6164 (DE-627)129170690 (DE-600)50983-8 (DE-576)01445520X 0743-7463 nnns volume:31 year:2015 number:22 pages:6164 http://www.ncbi.nlm.nih.gov/pubmed/25978768 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_23 GBV_ILN_70 GBV_ILN_2006 GBV_ILN_2007 VA 5760 35.18 AVZ AR 31 2015 22 6164
allfields_unstemmed	PQ20160617 (DE-627)OLC1957081163 (DE-599)GBVOLC1957081163 (PRQ)p834-cf0d66cce5e091e4d49f73e62927f6cbb9b8a7266b994eb02f47b211774c1f5b0 (KEY)0138429520150000031002206164atomicforcemicroscopyrevealsthemechanobiologyoflyt DE-627 ger DE-627 rakwb eng 670 540 DE-600 VA 5760 AVZ rvk 35.18 bkl Mularski, Anna verfasserin aut Atomic Force Microscopy Reveals the Mechanobiology of Lytic Peptide Action on Bacteria 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Increasing rates of antimicrobial-resistant medically important bacteria require the development of new, effective therapeutics, of which antimicrobial peptides (AMPs) are among the promising candidates. Many AMPs are membrane-active, but their mode of action in killing bacteria or in inhibiting their growth remains elusive. This study used atomic force microscopy (AFM) to probe the mechanobiology of a model AMP (a derivative of melittin) on living Klebsiella pneumoniae bacterial cells. We performed in situ biophysical measurements to understand how the melittin peptide modulates various biophysical behaviors of individual bacteria, including the turgor pressure, cell wall elasticity, and bacterial capsule thickness and organization. Exposure of K. pneumoniae to the peptide had a significant effect on the turgor pressure and Young's modulus of the cell wall. The turgor pressure increased upon peptide addition followed by a later decrease, suggesting that cell lysis occurred and pressure was lost through destruction of the cell envelope. The Young's modulus also increased, indicating that interaction with the peptide increased the rigidity of the cell wall. The bacterial capsule did not prevent cell lysis by the peptide, and surprisingly, the capsule appeared unaffected by exposure to the peptide, as capsule thickness and inferred organization were within the control limits, determined by mechanical measurements. These data show that AFM measurements may provide valuable insights into the physical events that precede bacterial lysis by AMPs. Wilksch, Jonathan J oth Wang, Huabin oth Hossain, Mohammed Akhter oth Wade, John D oth Separovic, Frances oth Strugnell, Richard A oth Gee, Michelle L oth Enthalten in Langmuir Washington, DC : ACS Publ., 1985 31(2015), 22, Seite 6164 (DE-627)129170690 (DE-600)50983-8 (DE-576)01445520X 0743-7463 nnns volume:31 year:2015 number:22 pages:6164 http://www.ncbi.nlm.nih.gov/pubmed/25978768 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_23 GBV_ILN_70 GBV_ILN_2006 GBV_ILN_2007 VA 5760 35.18 AVZ AR 31 2015 22 6164
allfieldsGer	PQ20160617 (DE-627)OLC1957081163 (DE-599)GBVOLC1957081163 (PRQ)p834-cf0d66cce5e091e4d49f73e62927f6cbb9b8a7266b994eb02f47b211774c1f5b0 (KEY)0138429520150000031002206164atomicforcemicroscopyrevealsthemechanobiologyoflyt DE-627 ger DE-627 rakwb eng 670 540 DE-600 VA 5760 AVZ rvk 35.18 bkl Mularski, Anna verfasserin aut Atomic Force Microscopy Reveals the Mechanobiology of Lytic Peptide Action on Bacteria 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Increasing rates of antimicrobial-resistant medically important bacteria require the development of new, effective therapeutics, of which antimicrobial peptides (AMPs) are among the promising candidates. Many AMPs are membrane-active, but their mode of action in killing bacteria or in inhibiting their growth remains elusive. This study used atomic force microscopy (AFM) to probe the mechanobiology of a model AMP (a derivative of melittin) on living Klebsiella pneumoniae bacterial cells. We performed in situ biophysical measurements to understand how the melittin peptide modulates various biophysical behaviors of individual bacteria, including the turgor pressure, cell wall elasticity, and bacterial capsule thickness and organization. Exposure of K. pneumoniae to the peptide had a significant effect on the turgor pressure and Young's modulus of the cell wall. The turgor pressure increased upon peptide addition followed by a later decrease, suggesting that cell lysis occurred and pressure was lost through destruction of the cell envelope. The Young's modulus also increased, indicating that interaction with the peptide increased the rigidity of the cell wall. The bacterial capsule did not prevent cell lysis by the peptide, and surprisingly, the capsule appeared unaffected by exposure to the peptide, as capsule thickness and inferred organization were within the control limits, determined by mechanical measurements. These data show that AFM measurements may provide valuable insights into the physical events that precede bacterial lysis by AMPs. Wilksch, Jonathan J oth Wang, Huabin oth Hossain, Mohammed Akhter oth Wade, John D oth Separovic, Frances oth Strugnell, Richard A oth Gee, Michelle L oth Enthalten in Langmuir Washington, DC : ACS Publ., 1985 31(2015), 22, Seite 6164 (DE-627)129170690 (DE-600)50983-8 (DE-576)01445520X 0743-7463 nnns volume:31 year:2015 number:22 pages:6164 http://www.ncbi.nlm.nih.gov/pubmed/25978768 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_23 GBV_ILN_70 GBV_ILN_2006 GBV_ILN_2007 VA 5760 35.18 AVZ AR 31 2015 22 6164
allfieldsSound	PQ20160617 (DE-627)OLC1957081163 (DE-599)GBVOLC1957081163 (PRQ)p834-cf0d66cce5e091e4d49f73e62927f6cbb9b8a7266b994eb02f47b211774c1f5b0 (KEY)0138429520150000031002206164atomicforcemicroscopyrevealsthemechanobiologyoflyt DE-627 ger DE-627 rakwb eng 670 540 DE-600 VA 5760 AVZ rvk 35.18 bkl Mularski, Anna verfasserin aut Atomic Force Microscopy Reveals the Mechanobiology of Lytic Peptide Action on Bacteria 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Increasing rates of antimicrobial-resistant medically important bacteria require the development of new, effective therapeutics, of which antimicrobial peptides (AMPs) are among the promising candidates. Many AMPs are membrane-active, but their mode of action in killing bacteria or in inhibiting their growth remains elusive. This study used atomic force microscopy (AFM) to probe the mechanobiology of a model AMP (a derivative of melittin) on living Klebsiella pneumoniae bacterial cells. We performed in situ biophysical measurements to understand how the melittin peptide modulates various biophysical behaviors of individual bacteria, including the turgor pressure, cell wall elasticity, and bacterial capsule thickness and organization. Exposure of K. pneumoniae to the peptide had a significant effect on the turgor pressure and Young's modulus of the cell wall. The turgor pressure increased upon peptide addition followed by a later decrease, suggesting that cell lysis occurred and pressure was lost through destruction of the cell envelope. The Young's modulus also increased, indicating that interaction with the peptide increased the rigidity of the cell wall. The bacterial capsule did not prevent cell lysis by the peptide, and surprisingly, the capsule appeared unaffected by exposure to the peptide, as capsule thickness and inferred organization were within the control limits, determined by mechanical measurements. These data show that AFM measurements may provide valuable insights into the physical events that precede bacterial lysis by AMPs. Wilksch, Jonathan J oth Wang, Huabin oth Hossain, Mohammed Akhter oth Wade, John D oth Separovic, Frances oth Strugnell, Richard A oth Gee, Michelle L oth Enthalten in Langmuir Washington, DC : ACS Publ., 1985 31(2015), 22, Seite 6164 (DE-627)129170690 (DE-600)50983-8 (DE-576)01445520X 0743-7463 nnns volume:31 year:2015 number:22 pages:6164 http://www.ncbi.nlm.nih.gov/pubmed/25978768 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_23 GBV_ILN_70 GBV_ILN_2006 GBV_ILN_2007 VA 5760 35.18 AVZ AR 31 2015 22 6164
language	English
source	Enthalten in Langmuir 31(2015), 22, Seite 6164 volume:31 year:2015 number:22 pages:6164
sourceStr	Enthalten in Langmuir 31(2015), 22, Seite 6164 volume:31 year:2015 number:22 pages:6164
format_phy_str_mv	Article
institution	findex.gbv.de
dewey-raw	670
isfreeaccess_bool	false
container_title	Langmuir
authorswithroles_txt_mv	Mularski, Anna @@aut@@ Wilksch, Jonathan J @@oth@@ Wang, Huabin @@oth@@ Hossain, Mohammed Akhter @@oth@@ Wade, John D @@oth@@ Separovic, Frances @@oth@@ Strugnell, Richard A @@oth@@ Gee, Michelle L @@oth@@
publishDateDaySort_date	2015-01-01T00:00:00Z
hierarchy_top_id	129170690
dewey-sort	3670
id	OLC1957081163
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">OLC1957081163</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230515194422.0</controlfield><controlfield tag="007">tu</controlfield><controlfield tag="008">160206s2015 xx \|\|\|\|\| 00\| \|\|eng c</controlfield><datafield tag="028" ind1="5" ind2="2"><subfield code="a">PQ20160617</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)OLC1957081163</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVOLC1957081163</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(PRQ)p834-cf0d66cce5e091e4d49f73e62927f6cbb9b8a7266b994eb02f47b211774c1f5b0</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(KEY)0138429520150000031002206164atomicforcemicroscopyrevealsthemechanobiologyoflyt</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">670</subfield><subfield code="a">540</subfield><subfield code="q">DE-600</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">VA 5760</subfield><subfield code="q">AVZ</subfield><subfield code="2">rvk</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">35.18</subfield><subfield code="2">bkl</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Mularski, Anna</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Atomic Force Microscopy Reveals the Mechanobiology of Lytic Peptide Action on Bacteria</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2015</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">Increasing rates of antimicrobial-resistant medically important bacteria require the development of new, effective therapeutics, of which antimicrobial peptides (AMPs) are among the promising candidates. Many AMPs are membrane-active, but their mode of action in killing bacteria or in inhibiting their growth remains elusive. This study used atomic force microscopy (AFM) to probe the mechanobiology of a model AMP (a derivative of melittin) on living Klebsiella pneumoniae bacterial cells. We performed in situ biophysical measurements to understand how the melittin peptide modulates various biophysical behaviors of individual bacteria, including the turgor pressure, cell wall elasticity, and bacterial capsule thickness and organization. Exposure of K. pneumoniae to the peptide had a significant effect on the turgor pressure and Young's modulus of the cell wall. The turgor pressure increased upon peptide addition followed by a later decrease, suggesting that cell lysis occurred and pressure was lost through destruction of the cell envelope. The Young's modulus also increased, indicating that interaction with the peptide increased the rigidity of the cell wall. The bacterial capsule did not prevent cell lysis by the peptide, and surprisingly, the capsule appeared unaffected by exposure to the peptide, as capsule thickness and inferred organization were within the control limits, determined by mechanical measurements. These data show that AFM measurements may provide valuable insights into the physical events that precede bacterial lysis by AMPs.</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Wilksch, Jonathan J</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Wang, Huabin</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Hossain, Mohammed Akhter</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Wade, John D</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Separovic, Frances</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Strugnell, Richard A</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Gee, Michelle L</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">Langmuir</subfield><subfield code="d">Washington, DC : ACS Publ., 1985</subfield><subfield code="g">31(2015), 22, Seite 6164</subfield><subfield code="w">(DE-627)129170690</subfield><subfield code="w">(DE-600)50983-8</subfield><subfield code="w">(DE-576)01445520X</subfield><subfield code="x">0743-7463</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:31</subfield><subfield code="g">year:2015</subfield><subfield code="g">number:22</subfield><subfield code="g">pages:6164</subfield></datafield><datafield tag="856" ind1="4" ind2="2"><subfield code="u">http://www.ncbi.nlm.nih.gov/pubmed/25978768</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">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">SSG-OLC-PHA</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-DE-84</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_23</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_2006</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2007</subfield></datafield><datafield tag="936" ind1="r" ind2="v"><subfield code="a">VA 5760</subfield></datafield><datafield tag="936" ind1="b" ind2="k"><subfield code="a">35.18</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">31</subfield><subfield code="j">2015</subfield><subfield code="e">22</subfield><subfield code="h">6164</subfield></datafield></record></collection>
author	Mularski, Anna
spellingShingle	Mularski, Anna ddc 670 rvk VA 5760 bkl 35.18 Atomic Force Microscopy Reveals the Mechanobiology of Lytic Peptide Action on Bacteria
authorStr	Mularski, Anna
ppnlink_with_tag_str_mv	@@773@@(DE-627)129170690
format	Article
dewey-ones	670 - Manufacturing 540 - Chemistry & allied sciences
delete_txt_mv	keep
author_role	aut
collection	OLC
remote_str	false
illustrated	Not Illustrated
issn	0743-7463
topic_title	670 540 DE-600 VA 5760 AVZ rvk 35.18 bkl Atomic Force Microscopy Reveals the Mechanobiology of Lytic Peptide Action on Bacteria
topic	ddc 670 rvk VA 5760 bkl 35.18
topic_unstemmed	ddc 670 rvk VA 5760 bkl 35.18
topic_browse	ddc 670 rvk VA 5760 bkl 35.18
format_facet	Aufsätze Gedruckte Aufsätze
format_main_str_mv	Text Zeitschrift/Artikel
carriertype_str_mv	nc
author2_variant	j j w jj jjw h w hw m a h ma mah j d w jd jdw f s fs r a s ra ras m l g ml mlg
hierarchy_parent_title	Langmuir
hierarchy_parent_id	129170690
dewey-tens	670 - Manufacturing 540 - Chemistry
hierarchy_top_title	Langmuir
isfreeaccess_txt	false
familylinks_str_mv	(DE-627)129170690 (DE-600)50983-8 (DE-576)01445520X
title	Atomic Force Microscopy Reveals the Mechanobiology of Lytic Peptide Action on Bacteria
ctrlnum	(DE-627)OLC1957081163 (DE-599)GBVOLC1957081163 (PRQ)p834-cf0d66cce5e091e4d49f73e62927f6cbb9b8a7266b994eb02f47b211774c1f5b0 (KEY)0138429520150000031002206164atomicforcemicroscopyrevealsthemechanobiologyoflyt
title_full	Atomic Force Microscopy Reveals the Mechanobiology of Lytic Peptide Action on Bacteria
author_sort	Mularski, Anna
journal	Langmuir
journalStr	Langmuir
lang_code	eng
isOA_bool	false
dewey-hundreds	600 - Technology 500 - Science
recordtype	marc
publishDateSort	2015
contenttype_str_mv	txt
container_start_page	6164
author_browse	Mularski, Anna
container_volume	31
class	670 540 DE-600 VA 5760 AVZ rvk 35.18 bkl
format_se	Aufsätze
author-letter	Mularski, Anna
dewey-full	670 540
title_sort	atomic force microscopy reveals the mechanobiology of lytic peptide action on bacteria
title_auth	Atomic Force Microscopy Reveals the Mechanobiology of Lytic Peptide Action on Bacteria
abstract	Increasing rates of antimicrobial-resistant medically important bacteria require the development of new, effective therapeutics, of which antimicrobial peptides (AMPs) are among the promising candidates. Many AMPs are membrane-active, but their mode of action in killing bacteria or in inhibiting their growth remains elusive. This study used atomic force microscopy (AFM) to probe the mechanobiology of a model AMP (a derivative of melittin) on living Klebsiella pneumoniae bacterial cells. We performed in situ biophysical measurements to understand how the melittin peptide modulates various biophysical behaviors of individual bacteria, including the turgor pressure, cell wall elasticity, and bacterial capsule thickness and organization. Exposure of K. pneumoniae to the peptide had a significant effect on the turgor pressure and Young's modulus of the cell wall. The turgor pressure increased upon peptide addition followed by a later decrease, suggesting that cell lysis occurred and pressure was lost through destruction of the cell envelope. The Young's modulus also increased, indicating that interaction with the peptide increased the rigidity of the cell wall. The bacterial capsule did not prevent cell lysis by the peptide, and surprisingly, the capsule appeared unaffected by exposure to the peptide, as capsule thickness and inferred organization were within the control limits, determined by mechanical measurements. These data show that AFM measurements may provide valuable insights into the physical events that precede bacterial lysis by AMPs.
abstractGer	Increasing rates of antimicrobial-resistant medically important bacteria require the development of new, effective therapeutics, of which antimicrobial peptides (AMPs) are among the promising candidates. Many AMPs are membrane-active, but their mode of action in killing bacteria or in inhibiting their growth remains elusive. This study used atomic force microscopy (AFM) to probe the mechanobiology of a model AMP (a derivative of melittin) on living Klebsiella pneumoniae bacterial cells. We performed in situ biophysical measurements to understand how the melittin peptide modulates various biophysical behaviors of individual bacteria, including the turgor pressure, cell wall elasticity, and bacterial capsule thickness and organization. Exposure of K. pneumoniae to the peptide had a significant effect on the turgor pressure and Young's modulus of the cell wall. The turgor pressure increased upon peptide addition followed by a later decrease, suggesting that cell lysis occurred and pressure was lost through destruction of the cell envelope. The Young's modulus also increased, indicating that interaction with the peptide increased the rigidity of the cell wall. The bacterial capsule did not prevent cell lysis by the peptide, and surprisingly, the capsule appeared unaffected by exposure to the peptide, as capsule thickness and inferred organization were within the control limits, determined by mechanical measurements. These data show that AFM measurements may provide valuable insights into the physical events that precede bacterial lysis by AMPs.
abstract_unstemmed	Increasing rates of antimicrobial-resistant medically important bacteria require the development of new, effective therapeutics, of which antimicrobial peptides (AMPs) are among the promising candidates. Many AMPs are membrane-active, but their mode of action in killing bacteria or in inhibiting their growth remains elusive. This study used atomic force microscopy (AFM) to probe the mechanobiology of a model AMP (a derivative of melittin) on living Klebsiella pneumoniae bacterial cells. We performed in situ biophysical measurements to understand how the melittin peptide modulates various biophysical behaviors of individual bacteria, including the turgor pressure, cell wall elasticity, and bacterial capsule thickness and organization. Exposure of K. pneumoniae to the peptide had a significant effect on the turgor pressure and Young's modulus of the cell wall. The turgor pressure increased upon peptide addition followed by a later decrease, suggesting that cell lysis occurred and pressure was lost through destruction of the cell envelope. The Young's modulus also increased, indicating that interaction with the peptide increased the rigidity of the cell wall. The bacterial capsule did not prevent cell lysis by the peptide, and surprisingly, the capsule appeared unaffected by exposure to the peptide, as capsule thickness and inferred organization were within the control limits, determined by mechanical measurements. These data show that AFM measurements may provide valuable insights into the physical events that precede bacterial lysis by AMPs.
collection_details	GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_23 GBV_ILN_70 GBV_ILN_2006 GBV_ILN_2007
container_issue	22
title_short	Atomic Force Microscopy Reveals the Mechanobiology of Lytic Peptide Action on Bacteria
url	http://www.ncbi.nlm.nih.gov/pubmed/25978768
remote_bool	false
author2	Wilksch, Jonathan J Wang, Huabin Hossain, Mohammed Akhter Wade, John D Separovic, Frances Strugnell, Richard A Gee, Michelle L
author2Str	Wilksch, Jonathan J Wang, Huabin Hossain, Mohammed Akhter Wade, John D Separovic, Frances Strugnell, Richard A Gee, Michelle L
ppnlink	129170690
mediatype_str_mv	n
isOA_txt	false
hochschulschrift_bool	false
author2_role	oth oth oth oth oth oth oth
up_date	2024-07-03T23:07:04.702Z
_version_	1803601077553070080
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">OLC1957081163</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230515194422.0</controlfield><controlfield tag="007">tu</controlfield><controlfield tag="008">160206s2015 xx \|\|\|\|\| 00\| \|\|eng c</controlfield><datafield tag="028" ind1="5" ind2="2"><subfield code="a">PQ20160617</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)OLC1957081163</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVOLC1957081163</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(PRQ)p834-cf0d66cce5e091e4d49f73e62927f6cbb9b8a7266b994eb02f47b211774c1f5b0</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(KEY)0138429520150000031002206164atomicforcemicroscopyrevealsthemechanobiologyoflyt</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">670</subfield><subfield code="a">540</subfield><subfield code="q">DE-600</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">VA 5760</subfield><subfield code="q">AVZ</subfield><subfield code="2">rvk</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">35.18</subfield><subfield code="2">bkl</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Mularski, Anna</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Atomic Force Microscopy Reveals the Mechanobiology of Lytic Peptide Action on Bacteria</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2015</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">Increasing rates of antimicrobial-resistant medically important bacteria require the development of new, effective therapeutics, of which antimicrobial peptides (AMPs) are among the promising candidates. Many AMPs are membrane-active, but their mode of action in killing bacteria or in inhibiting their growth remains elusive. This study used atomic force microscopy (AFM) to probe the mechanobiology of a model AMP (a derivative of melittin) on living Klebsiella pneumoniae bacterial cells. We performed in situ biophysical measurements to understand how the melittin peptide modulates various biophysical behaviors of individual bacteria, including the turgor pressure, cell wall elasticity, and bacterial capsule thickness and organization. Exposure of K. pneumoniae to the peptide had a significant effect on the turgor pressure and Young's modulus of the cell wall. The turgor pressure increased upon peptide addition followed by a later decrease, suggesting that cell lysis occurred and pressure was lost through destruction of the cell envelope. The Young's modulus also increased, indicating that interaction with the peptide increased the rigidity of the cell wall. The bacterial capsule did not prevent cell lysis by the peptide, and surprisingly, the capsule appeared unaffected by exposure to the peptide, as capsule thickness and inferred organization were within the control limits, determined by mechanical measurements. These data show that AFM measurements may provide valuable insights into the physical events that precede bacterial lysis by AMPs.</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Wilksch, Jonathan J</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Wang, Huabin</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Hossain, Mohammed Akhter</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Wade, John D</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Separovic, Frances</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Strugnell, Richard A</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Gee, Michelle L</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">Langmuir</subfield><subfield code="d">Washington, DC : ACS Publ., 1985</subfield><subfield code="g">31(2015), 22, Seite 6164</subfield><subfield code="w">(DE-627)129170690</subfield><subfield code="w">(DE-600)50983-8</subfield><subfield code="w">(DE-576)01445520X</subfield><subfield code="x">0743-7463</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:31</subfield><subfield code="g">year:2015</subfield><subfield code="g">number:22</subfield><subfield code="g">pages:6164</subfield></datafield><datafield tag="856" ind1="4" ind2="2"><subfield code="u">http://www.ncbi.nlm.nih.gov/pubmed/25978768</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">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">SSG-OLC-PHA</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-DE-84</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_23</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_2006</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2007</subfield></datafield><datafield tag="936" ind1="r" ind2="v"><subfield code="a">VA 5760</subfield></datafield><datafield tag="936" ind1="b" ind2="k"><subfield code="a">35.18</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">31</subfield><subfield code="j">2015</subfield><subfield code="e">22</subfield><subfield code="h">6164</subfield></datafield></record></collection>
score	7.398486

Nicht das Richtige dabei?

Schreiben Sie uns!

Atomic Force Microscopy Reveals the Mechanobiology of Lytic Peptide Action on Bacteria

Nicht das Richtige dabei?

Zugang & Verfügbarkeit

Vorhandene Bände

Nicht das Richtige dabei?