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The effect of peptide glycation on protein secondary structure

Povey, Jane F., Howard, Mark J., Williamson, Richard A., Smales, Christopher Mark (2008) The effect of peptide glycation on protein secondary structure. Journal of Structural Biology, 161 (2). pp. 151-161. ISSN 1047-8477. (doi:10.1016/j.jsb.2007.10.004) (Access to this publication is currently restricted. You may be able to access a copy if URLs are provided) (KAR id:22662)

Language: English

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Protein glycation is a non-enzymatic reaction between reducing sugars and amino groups that occurs in vivo and has been implicated in a number of disease states and pathologies including Alzheimer's and diabetes. Although glycation is thought to alter protein structure and function, there is currently little information on the structural consequences of this modification. We have used a model alpha-helix and a model beta-hairpin peptide, and NMR analysis, to investigate the effects of glycation upon secondary structure. Glycation of the dilysine motif within the alpha-helix peptide occurred preferentially at one lysine residue and resulted in severe disruption to the local secondary structure. The area immediately around the site of modification was extremely flexible and the peptide did not adopt a preferred conformation in this area of the helix in 30% TFE. Significant glycation of the beta-hairpin peptide was not detected and the structure was unchanged. These results show that glycation results in local secondary structure distortion of alpha-helices and that preferential glycation occurs in a sequence specific manner. The findings will allow us to interrogate the local environment in other peptides/proteins to predict the likelihood of glycation, and to model the potential effects such modification might have upon structure/function.

Item Type: Article
DOI/Identification number: 10.1016/j.jsb.2007.10.004
Additional information: 1095-8657 (Electronic) Journal Article Research Support, Non-U.S. Gov't
Uncontrolled keywords: Amino Acid Sequence, Glycosylation, Humans *Models Molecular, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular Peptides/*chemistry, Protein Structure, Secondary Tissue Inhibitor of Metalloproteinase-2/chemistry
Subjects: Q Science > QP Physiology (Living systems) > QP506 Molecular biology
Divisions: Divisions > Division of Natural Sciences > Biosciences
Depositing User: M.J. Howard
Date Deposited: 02 Oct 2009 14:37 UTC
Last Modified: 16 Nov 2021 10:01 UTC
Resource URI: (The current URI for this page, for reference purposes)
Smales, Christopher Mark:
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