Prolonged Glycation of Hen Egg White Lysozyme Generates Non Amyloidal Structures

Prolonged Glycation of Hen Egg White Lysozyme Generates Non Amyloidal Structures

Glycation causes severe damage to protein structure that could lead to amyloid formation in special cases. Here in this report, we have shown for the first time that hen egg white lysozyme (HEWL) does not undergo amyloid formation even after prolonged glycation in the presence of D-glucose, D-fructo...

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Main Authors: Ghosh, Sudeshna, Pandey, Nitin Kumar, Singha Roy, Atanu, Tripathy, Debi Ranjan, Dinda, Amit Kumar, Dasgupta, Swagata
Format: Online
Language:English
Published: Public Library of Science 2013
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3774808/
id pubmed-3774808
recordtype oai_dc
spelling pubmed-37748082013-09-24 Prolonged Glycation of Hen Egg White Lysozyme Generates Non Amyloidal Structures Ghosh, Sudeshna Pandey, Nitin Kumar Singha Roy, Atanu Tripathy, Debi Ranjan Dinda, Amit Kumar Dasgupta, Swagata Research Article Glycation causes severe damage to protein structure that could lead to amyloid formation in special cases. Here in this report, we have shown for the first time that hen egg white lysozyme (HEWL) does not undergo amyloid formation even after prolonged glycation in the presence of D-glucose, D-fructose and D-ribose. Cross-linked oligomers were formed in all the cases and ribose was found to be the most potent among the three sugars. Ribose mediated oligomers, however, exhibit Thioflavin T binding properties although microscopic images clearly show amorphous and globular morphology of the aggregates. Our study demonstrates that the structural damage of hen egg white lysozyme due to glycation generates unstructured aggregates. Public Library of Science 2013-09-16 /pmc/articles/PMC3774808/ /pubmed/24066139 http://dx.doi.org/10.1371/journal.pone.0074336 Text en © 2013 Ghosh et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
author Ghosh, Sudeshna
Pandey, Nitin Kumar
Singha Roy, Atanu
Tripathy, Debi Ranjan
Dinda, Amit Kumar
Dasgupta, Swagata
spellingShingle Ghosh, Sudeshna
Pandey, Nitin Kumar
Singha Roy, Atanu
Tripathy, Debi Ranjan
Dinda, Amit Kumar
Dasgupta, Swagata
Prolonged Glycation of Hen Egg White Lysozyme Generates Non Amyloidal Structures
author_facet Ghosh, Sudeshna
Pandey, Nitin Kumar
Singha Roy, Atanu
Tripathy, Debi Ranjan
Dinda, Amit Kumar
Dasgupta, Swagata
author_sort Ghosh, Sudeshna
title Prolonged Glycation of Hen Egg White Lysozyme Generates Non Amyloidal Structures
title_short Prolonged Glycation of Hen Egg White Lysozyme Generates Non Amyloidal Structures
title_full Prolonged Glycation of Hen Egg White Lysozyme Generates Non Amyloidal Structures
title_fullStr Prolonged Glycation of Hen Egg White Lysozyme Generates Non Amyloidal Structures
title_full_unstemmed Prolonged Glycation of Hen Egg White Lysozyme Generates Non Amyloidal Structures
title_sort prolonged glycation of hen egg white lysozyme generates non amyloidal structures
description Glycation causes severe damage to protein structure that could lead to amyloid formation in special cases. Here in this report, we have shown for the first time that hen egg white lysozyme (HEWL) does not undergo amyloid formation even after prolonged glycation in the presence of D-glucose, D-fructose and D-ribose. Cross-linked oligomers were formed in all the cases and ribose was found to be the most potent among the three sugars. Ribose mediated oligomers, however, exhibit Thioflavin T binding properties although microscopic images clearly show amorphous and globular morphology of the aggregates. Our study demonstrates that the structural damage of hen egg white lysozyme due to glycation generates unstructured aggregates.
publisher Public Library of Science
publishDate 2013
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3774808/
_version_ 1612011925833515008

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