Perez Hurtado, Pilar and O’Connor, Peter B.. (2012) Deamidation of collagen. Analytical Chemistry, Vol.84 (No.6). pp. 3017-3025. ISSN 0003-2700

Full text not available from this repository.

Abstract

Collagen is the major component of skin, tendons, ligaments, teeth, and bones, it provides the framework that holds most multicellular animals together, and collagen type I constitutes the major fibrillar collagen of bone. Because of the complexity of collagen’s structure, the study of post-translational modifications such as deamidation for this protein is challenging. Although there is no evidence of this protein being used for age assessment, it has been shown that deamidation of collagen is remarkably increased in old bones from mammals. Nonspectrometric methodologies have been used for the determination of the extent of deamidation as a measure of the amount of amide nitrogen released in ammonia as well as constant rates for deamidation of asparagine in collagen. In general, these methodologies required more sample and separation processes. To understand if collagen plays a significant role in the aging process of fossil materials, a simpler and more accurate method is needed to determine the extent of deamidation at the whole protein level. The present work shows a method to determine the extent of deamidation in collagen using Fourier transform ion cyclotron resonance-mass spectrometry (FTICR-MS) along with collisionally activated dissociation (CAD) and electron capture dissociation (ECD). The measured deamidation half-life for three different tryptic peptides from collagen (I) ranged from 2000 to 6000 s under high temperature conditions (62 °C) and pH 7.5.

Item Type:	Journal Article
Divisions:	Faculty of Science > Chemistry
Journal or Publication Title:	Analytical Chemistry
Publisher:	American Chemical Society
ISSN:	0003-2700
Date:	2012
Volume:	Vol.84
Number:	No.6
Page Range:	pp. 3017-3025
Identification Number:	10.1021/ac202980z
Status:	Peer Reviewed
Publication Status:	Published
Access rights to Published version:	Restricted or Subscription Access
URI:	http://wrap.warwick.ac.uk/id/eprint/48619

Request changes to a record

Actions (login required)

View Item