Distinct impact of glycation towards the aggregation and toxicity of murine and human amyloid-β

Eunju Nam; Jiyeon Han; Sunhee Choi; Mi Hee Lim

doi:10.1039/d1cc02695j

Distinct impact of glycation towards the aggregation and toxicity of murine and human amyloid-β

Eunju Nam
, Jiyeon Han
, Sunhee Choi
, Mi Hee Lim

Department of Applied Chemistry

Korea Advanced Institute of Science and Technology
Middlebury College

Research output: Contribution to journal › Article › peer-review

5 Scopus citations

Abstract

Glycation of human Aβ (hAβ) is implicated to induce the deposition of amyloid aggregates found in the Alzheimer's disease (AD)-affected brain. Murine Aβ (mAβ) differs from hAβ in three different amino acid residues (Gly5, Phe10, and Arg13) and is less likely to form amyloid aggregates. Herein, we report that the advanced glycated end products of mAβ₄₀over hAβ₄₀are distinctly generated. The different glycation between the two peptides can govern their aggregation kinetics, structural transition, and cytotoxicity.

Original language	English
Pages (from-to)	7637-7640
Number of pages	4
Journal	Chemical Communications
Volume	57
Issue number	62
DOIs	https://doi.org/10.1039/d1cc02695j
State	Published - 11 Aug 2021

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abstract = "Glycation of human Aβ (hAβ) is implicated to induce the deposition of amyloid aggregates found in the Alzheimer's disease (AD)-affected brain. Murine Aβ (mAβ) differs from hAβ in three different amino acid residues (Gly5, Phe10, and Arg13) and is less likely to form amyloid aggregates. Herein, we report that the advanced glycated end products of mAβ40over hAβ40are distinctly generated. The different glycation between the two peptides can govern their aggregation kinetics, structural transition, and cytotoxicity.",

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AU - Choi, Sunhee

AU - Lim, Mi Hee

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Y1 - 2021/8/11

N2 - Glycation of human Aβ (hAβ) is implicated to induce the deposition of amyloid aggregates found in the Alzheimer's disease (AD)-affected brain. Murine Aβ (mAβ) differs from hAβ in three different amino acid residues (Gly5, Phe10, and Arg13) and is less likely to form amyloid aggregates. Herein, we report that the advanced glycated end products of mAβ40over hAβ40are distinctly generated. The different glycation between the two peptides can govern their aggregation kinetics, structural transition, and cytotoxicity.

AB - Glycation of human Aβ (hAβ) is implicated to induce the deposition of amyloid aggregates found in the Alzheimer's disease (AD)-affected brain. Murine Aβ (mAβ) differs from hAβ in three different amino acid residues (Gly5, Phe10, and Arg13) and is less likely to form amyloid aggregates. Herein, we report that the advanced glycated end products of mAβ40over hAβ40are distinctly generated. The different glycation between the two peptides can govern their aggregation kinetics, structural transition, and cytotoxicity.

UR - https://www.scopus.com/pages/publications/85111911843

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DO - 10.1039/d1cc02695j

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JF - Chemical Communications

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ER -

Distinct impact of glycation towards the aggregation and toxicity of murine and human amyloid-β

Abstract

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