Very small changes in the peptide sequence alter the redox properties of Aβ(11–16)-Cu(II) and pAβ(11–16)-Cu(II) β-amyloid complexes

Alzheimer’s disease is the most common neurodegenerative disease in the world and oxidative stress is a major factor in its pathogenesis. It is known that copper(II) ions forming complexes with peptides from the β-amyloid (Aβ) group can facilitate the production of reactive oxygen species. A very co...
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Gespeichert in:

Autor*in:	Wiloch, Magdalena Z. [verfasserIn] Jönsson-Niedziółka, Martin [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2022

Schlagwörter:	Alzheimer’s disease Amyloid-β peptides Voltammetry Copper complexes Pyroglutamate-modified Aβ

Übergeordnetes Werk:	Enthalten in: Journal of electroanalytical chemistry - New York, NY [u.a.] : Elsevier, 1959, 922
Übergeordnetes Werk:	volume:922

DOI / URN:	10.1016/j.jelechem.2022.116746

Katalog-ID:	ELV008527172

Internformat


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245	1	0	\|a Very small changes in the peptide sequence alter the redox properties of Aβ(11–16)-Cu(II) and pAβ(11–16)-Cu(II) β-amyloid complexes
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520			\|a Alzheimer’s disease is the most common neurodegenerative disease in the world and oxidative stress is a major factor in its pathogenesis. It is known that copper(II) ions forming complexes with peptides from the β-amyloid (Aβ) group can facilitate the production of reactive oxygen species. A very common amyloid in AD brain plaques Aβ(11–42) form very stable Cu(II)-complexes that suppress ROS formation. However, when glutamic acid in Aβ(11–42) undergoes dehydration form cyclic pyroglutamate, resulting in a new derivative pAβ(11–42), the Cu(II) stabilisation is much weaker. Here, we investigate, for the first time, the redox chemistry of pAβ(11–16)-Cu‑(II) complexes as a model system for pAβ(11–42). We show that the weaker Cu(II) affinity for the pyroglutamate-modified peptide leads to Cu(I)/Cu(II) oxidation at potentials associated with increased ROS production. Our study also shows a significant difference in the redox properties of the complex if phosphate ions are present in the electrolyte, underlining the importance of proper choice of buffer solutions. These results can be crucial for an increased understanding of AD pathogenesis.
650		4	\|a Alzheimer’s disease
650		4	\|a Amyloid-β peptides
650		4	\|a Voltammetry
650		4	\|a Copper complexes
650		4	\|a Pyroglutamate-modified Aβ
700	1		\|a Jönsson-Niedziółka, Martin \|e verfasserin \|4 aut
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author_variant	m z w mz mzw m j n mjn
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publishDate	2022
allfields	10.1016/j.jelechem.2022.116746 doi (DE-627)ELV008527172 (ELSEVIER)S1572-6657(22)00738-X DE-627 ger DE-627 rda eng 540 620 DE-600 35.27 bkl Wiloch, Magdalena Z. verfasserin (orcid)0000-0001-8331-8572 aut Very small changes in the peptide sequence alter the redox properties of Aβ(11–16)-Cu(II) and pAβ(11–16)-Cu(II) β-amyloid complexes 2022 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Alzheimer’s disease is the most common neurodegenerative disease in the world and oxidative stress is a major factor in its pathogenesis. It is known that copper(II) ions forming complexes with peptides from the β-amyloid (Aβ) group can facilitate the production of reactive oxygen species. A very common amyloid in AD brain plaques Aβ(11–42) form very stable Cu(II)-complexes that suppress ROS formation. However, when glutamic acid in Aβ(11–42) undergoes dehydration form cyclic pyroglutamate, resulting in a new derivative pAβ(11–42), the Cu(II) stabilisation is much weaker. Here, we investigate, for the first time, the redox chemistry of pAβ(11–16)-Cu‑(II) complexes as a model system for pAβ(11–42). We show that the weaker Cu(II) affinity for the pyroglutamate-modified peptide leads to Cu(I)/Cu(II) oxidation at potentials associated with increased ROS production. Our study also shows a significant difference in the redox properties of the complex if phosphate ions are present in the electrolyte, underlining the importance of proper choice of buffer solutions. These results can be crucial for an increased understanding of AD pathogenesis. Alzheimer’s disease Amyloid-β peptides Voltammetry Copper complexes Pyroglutamate-modified Aβ Jönsson-Niedziółka, Martin verfasserin aut Enthalten in Journal of electroanalytical chemistry New York, NY [u.a.] : Elsevier, 1959 922 Online-Ressource (DE-627)302466533 (DE-600)1491150-4 (DE-576)098614797 1873-2569 nnns volume:922 GBV_USEFLAG_U SYSFLAG_U GBV_ELV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 35.27 Elektrochemische Analyse AR 922
spelling	10.1016/j.jelechem.2022.116746 doi (DE-627)ELV008527172 (ELSEVIER)S1572-6657(22)00738-X DE-627 ger DE-627 rda eng 540 620 DE-600 35.27 bkl Wiloch, Magdalena Z. verfasserin (orcid)0000-0001-8331-8572 aut Very small changes in the peptide sequence alter the redox properties of Aβ(11–16)-Cu(II) and pAβ(11–16)-Cu(II) β-amyloid complexes 2022 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Alzheimer’s disease is the most common neurodegenerative disease in the world and oxidative stress is a major factor in its pathogenesis. It is known that copper(II) ions forming complexes with peptides from the β-amyloid (Aβ) group can facilitate the production of reactive oxygen species. A very common amyloid in AD brain plaques Aβ(11–42) form very stable Cu(II)-complexes that suppress ROS formation. However, when glutamic acid in Aβ(11–42) undergoes dehydration form cyclic pyroglutamate, resulting in a new derivative pAβ(11–42), the Cu(II) stabilisation is much weaker. Here, we investigate, for the first time, the redox chemistry of pAβ(11–16)-Cu‑(II) complexes as a model system for pAβ(11–42). We show that the weaker Cu(II) affinity for the pyroglutamate-modified peptide leads to Cu(I)/Cu(II) oxidation at potentials associated with increased ROS production. Our study also shows a significant difference in the redox properties of the complex if phosphate ions are present in the electrolyte, underlining the importance of proper choice of buffer solutions. These results can be crucial for an increased understanding of AD pathogenesis. Alzheimer’s disease Amyloid-β peptides Voltammetry Copper complexes Pyroglutamate-modified Aβ Jönsson-Niedziółka, Martin verfasserin aut Enthalten in Journal of electroanalytical chemistry New York, NY [u.a.] : Elsevier, 1959 922 Online-Ressource (DE-627)302466533 (DE-600)1491150-4 (DE-576)098614797 1873-2569 nnns volume:922 GBV_USEFLAG_U SYSFLAG_U GBV_ELV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 35.27 Elektrochemische Analyse AR 922
allfields_unstemmed	10.1016/j.jelechem.2022.116746 doi (DE-627)ELV008527172 (ELSEVIER)S1572-6657(22)00738-X DE-627 ger DE-627 rda eng 540 620 DE-600 35.27 bkl Wiloch, Magdalena Z. verfasserin (orcid)0000-0001-8331-8572 aut Very small changes in the peptide sequence alter the redox properties of Aβ(11–16)-Cu(II) and pAβ(11–16)-Cu(II) β-amyloid complexes 2022 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Alzheimer’s disease is the most common neurodegenerative disease in the world and oxidative stress is a major factor in its pathogenesis. It is known that copper(II) ions forming complexes with peptides from the β-amyloid (Aβ) group can facilitate the production of reactive oxygen species. A very common amyloid in AD brain plaques Aβ(11–42) form very stable Cu(II)-complexes that suppress ROS formation. However, when glutamic acid in Aβ(11–42) undergoes dehydration form cyclic pyroglutamate, resulting in a new derivative pAβ(11–42), the Cu(II) stabilisation is much weaker. Here, we investigate, for the first time, the redox chemistry of pAβ(11–16)-Cu‑(II) complexes as a model system for pAβ(11–42). We show that the weaker Cu(II) affinity for the pyroglutamate-modified peptide leads to Cu(I)/Cu(II) oxidation at potentials associated with increased ROS production. Our study also shows a significant difference in the redox properties of the complex if phosphate ions are present in the electrolyte, underlining the importance of proper choice of buffer solutions. These results can be crucial for an increased understanding of AD pathogenesis. Alzheimer’s disease Amyloid-β peptides Voltammetry Copper complexes Pyroglutamate-modified Aβ Jönsson-Niedziółka, Martin verfasserin aut Enthalten in Journal of electroanalytical chemistry New York, NY [u.a.] : Elsevier, 1959 922 Online-Ressource (DE-627)302466533 (DE-600)1491150-4 (DE-576)098614797 1873-2569 nnns volume:922 GBV_USEFLAG_U SYSFLAG_U GBV_ELV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 35.27 Elektrochemische Analyse AR 922
allfieldsGer	10.1016/j.jelechem.2022.116746 doi (DE-627)ELV008527172 (ELSEVIER)S1572-6657(22)00738-X DE-627 ger DE-627 rda eng 540 620 DE-600 35.27 bkl Wiloch, Magdalena Z. verfasserin (orcid)0000-0001-8331-8572 aut Very small changes in the peptide sequence alter the redox properties of Aβ(11–16)-Cu(II) and pAβ(11–16)-Cu(II) β-amyloid complexes 2022 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Alzheimer’s disease is the most common neurodegenerative disease in the world and oxidative stress is a major factor in its pathogenesis. It is known that copper(II) ions forming complexes with peptides from the β-amyloid (Aβ) group can facilitate the production of reactive oxygen species. A very common amyloid in AD brain plaques Aβ(11–42) form very stable Cu(II)-complexes that suppress ROS formation. However, when glutamic acid in Aβ(11–42) undergoes dehydration form cyclic pyroglutamate, resulting in a new derivative pAβ(11–42), the Cu(II) stabilisation is much weaker. Here, we investigate, for the first time, the redox chemistry of pAβ(11–16)-Cu‑(II) complexes as a model system for pAβ(11–42). We show that the weaker Cu(II) affinity for the pyroglutamate-modified peptide leads to Cu(I)/Cu(II) oxidation at potentials associated with increased ROS production. Our study also shows a significant difference in the redox properties of the complex if phosphate ions are present in the electrolyte, underlining the importance of proper choice of buffer solutions. These results can be crucial for an increased understanding of AD pathogenesis. Alzheimer’s disease Amyloid-β peptides Voltammetry Copper complexes Pyroglutamate-modified Aβ Jönsson-Niedziółka, Martin verfasserin aut Enthalten in Journal of electroanalytical chemistry New York, NY [u.a.] : Elsevier, 1959 922 Online-Ressource (DE-627)302466533 (DE-600)1491150-4 (DE-576)098614797 1873-2569 nnns volume:922 GBV_USEFLAG_U SYSFLAG_U GBV_ELV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 35.27 Elektrochemische Analyse AR 922
allfieldsSound	10.1016/j.jelechem.2022.116746 doi (DE-627)ELV008527172 (ELSEVIER)S1572-6657(22)00738-X DE-627 ger DE-627 rda eng 540 620 DE-600 35.27 bkl Wiloch, Magdalena Z. verfasserin (orcid)0000-0001-8331-8572 aut Very small changes in the peptide sequence alter the redox properties of Aβ(11–16)-Cu(II) and pAβ(11–16)-Cu(II) β-amyloid complexes 2022 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Alzheimer’s disease is the most common neurodegenerative disease in the world and oxidative stress is a major factor in its pathogenesis. It is known that copper(II) ions forming complexes with peptides from the β-amyloid (Aβ) group can facilitate the production of reactive oxygen species. A very common amyloid in AD brain plaques Aβ(11–42) form very stable Cu(II)-complexes that suppress ROS formation. However, when glutamic acid in Aβ(11–42) undergoes dehydration form cyclic pyroglutamate, resulting in a new derivative pAβ(11–42), the Cu(II) stabilisation is much weaker. Here, we investigate, for the first time, the redox chemistry of pAβ(11–16)-Cu‑(II) complexes as a model system for pAβ(11–42). We show that the weaker Cu(II) affinity for the pyroglutamate-modified peptide leads to Cu(I)/Cu(II) oxidation at potentials associated with increased ROS production. Our study also shows a significant difference in the redox properties of the complex if phosphate ions are present in the electrolyte, underlining the importance of proper choice of buffer solutions. These results can be crucial for an increased understanding of AD pathogenesis. Alzheimer’s disease Amyloid-β peptides Voltammetry Copper complexes Pyroglutamate-modified Aβ Jönsson-Niedziółka, Martin verfasserin aut Enthalten in Journal of electroanalytical chemistry New York, NY [u.a.] : Elsevier, 1959 922 Online-Ressource (DE-627)302466533 (DE-600)1491150-4 (DE-576)098614797 1873-2569 nnns volume:922 GBV_USEFLAG_U SYSFLAG_U GBV_ELV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 35.27 Elektrochemische Analyse AR 922
language	English
source	Enthalten in Journal of electroanalytical chemistry 922 volume:922
sourceStr	Enthalten in Journal of electroanalytical chemistry 922 volume:922
format_phy_str_mv	Article
bklname	Elektrochemische Analyse
institution	findex.gbv.de
topic_facet	Alzheimer’s disease Amyloid-β peptides Voltammetry Copper complexes Pyroglutamate-modified Aβ
dewey-raw	540
isfreeaccess_bool	false
container_title	Journal of electroanalytical chemistry
authorswithroles_txt_mv	Wiloch, Magdalena Z. @@aut@@ Jönsson-Niedziółka, Martin @@aut@@
publishDateDaySort_date	2022-01-01T00:00:00Z
hierarchy_top_id	302466533
dewey-sort	3540
id	ELV008527172
language_de	englisch
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author	Wiloch, Magdalena Z.
spellingShingle	Wiloch, Magdalena Z. ddc 540 bkl 35.27 misc Alzheimer’s disease misc Amyloid-β peptides misc Voltammetry misc Copper complexes misc Pyroglutamate-modified Aβ Very small changes in the peptide sequence alter the redox properties of Aβ(11–16)-Cu(II) and pAβ(11–16)-Cu(II) β-amyloid complexes
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topic_title	540 620 DE-600 35.27 bkl Very small changes in the peptide sequence alter the redox properties of Aβ(11–16)-Cu(II) and pAβ(11–16)-Cu(II) β-amyloid complexes Alzheimer’s disease Amyloid-β peptides Voltammetry Copper complexes Pyroglutamate-modified Aβ
topic	ddc 540 bkl 35.27 misc Alzheimer’s disease misc Amyloid-β peptides misc Voltammetry misc Copper complexes misc Pyroglutamate-modified Aβ
topic_unstemmed	ddc 540 bkl 35.27 misc Alzheimer’s disease misc Amyloid-β peptides misc Voltammetry misc Copper complexes misc Pyroglutamate-modified Aβ
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title	Very small changes in the peptide sequence alter the redox properties of Aβ(11–16)-Cu(II) and pAβ(11–16)-Cu(II) β-amyloid complexes
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title_full	Very small changes in the peptide sequence alter the redox properties of Aβ(11–16)-Cu(II) and pAβ(11–16)-Cu(II) β-amyloid complexes
author_sort	Wiloch, Magdalena Z.
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author_browse	Wiloch, Magdalena Z. Jönsson-Niedziółka, Martin
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author-letter	Wiloch, Magdalena Z.
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title_sort	very small changes in the peptide sequence alter the redox properties of aβ(11–16)-cu(ii) and paβ(11–16)-cu(ii) β-amyloid complexes
title_auth	Very small changes in the peptide sequence alter the redox properties of Aβ(11–16)-Cu(II) and pAβ(11–16)-Cu(II) β-amyloid complexes
abstract	Alzheimer’s disease is the most common neurodegenerative disease in the world and oxidative stress is a major factor in its pathogenesis. It is known that copper(II) ions forming complexes with peptides from the β-amyloid (Aβ) group can facilitate the production of reactive oxygen species. A very common amyloid in AD brain plaques Aβ(11–42) form very stable Cu(II)-complexes that suppress ROS formation. However, when glutamic acid in Aβ(11–42) undergoes dehydration form cyclic pyroglutamate, resulting in a new derivative pAβ(11–42), the Cu(II) stabilisation is much weaker. Here, we investigate, for the first time, the redox chemistry of pAβ(11–16)-Cu‑(II) complexes as a model system for pAβ(11–42). We show that the weaker Cu(II) affinity for the pyroglutamate-modified peptide leads to Cu(I)/Cu(II) oxidation at potentials associated with increased ROS production. Our study also shows a significant difference in the redox properties of the complex if phosphate ions are present in the electrolyte, underlining the importance of proper choice of buffer solutions. These results can be crucial for an increased understanding of AD pathogenesis.
abstractGer	Alzheimer’s disease is the most common neurodegenerative disease in the world and oxidative stress is a major factor in its pathogenesis. It is known that copper(II) ions forming complexes with peptides from the β-amyloid (Aβ) group can facilitate the production of reactive oxygen species. A very common amyloid in AD brain plaques Aβ(11–42) form very stable Cu(II)-complexes that suppress ROS formation. However, when glutamic acid in Aβ(11–42) undergoes dehydration form cyclic pyroglutamate, resulting in a new derivative pAβ(11–42), the Cu(II) stabilisation is much weaker. Here, we investigate, for the first time, the redox chemistry of pAβ(11–16)-Cu‑(II) complexes as a model system for pAβ(11–42). We show that the weaker Cu(II) affinity for the pyroglutamate-modified peptide leads to Cu(I)/Cu(II) oxidation at potentials associated with increased ROS production. Our study also shows a significant difference in the redox properties of the complex if phosphate ions are present in the electrolyte, underlining the importance of proper choice of buffer solutions. These results can be crucial for an increased understanding of AD pathogenesis.
abstract_unstemmed	Alzheimer’s disease is the most common neurodegenerative disease in the world and oxidative stress is a major factor in its pathogenesis. It is known that copper(II) ions forming complexes with peptides from the β-amyloid (Aβ) group can facilitate the production of reactive oxygen species. A very common amyloid in AD brain plaques Aβ(11–42) form very stable Cu(II)-complexes that suppress ROS formation. However, when glutamic acid in Aβ(11–42) undergoes dehydration form cyclic pyroglutamate, resulting in a new derivative pAβ(11–42), the Cu(II) stabilisation is much weaker. Here, we investigate, for the first time, the redox chemistry of pAβ(11–16)-Cu‑(II) complexes as a model system for pAβ(11–42). We show that the weaker Cu(II) affinity for the pyroglutamate-modified peptide leads to Cu(I)/Cu(II) oxidation at potentials associated with increased ROS production. Our study also shows a significant difference in the redox properties of the complex if phosphate ions are present in the electrolyte, underlining the importance of proper choice of buffer solutions. These results can be crucial for an increased understanding of AD pathogenesis.
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title_short	Very small changes in the peptide sequence alter the redox properties of Aβ(11–16)-Cu(II) and pAβ(11–16)-Cu(II) β-amyloid complexes
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doi_str	10.1016/j.jelechem.2022.116746
up_date	2024-07-06T20:00:21.745Z
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Very small changes in the peptide sequence alter the redox properties of Aβ(11–16)-Cu(II) and pAβ(11–16)-Cu(II) β-amyloid complexes

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