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作 者:Yi Zhang Rafea Naffa Christopher J.Garvey Catherine A.Maidment Sujay Prabakar
机构地区:[1]Leather and Shoe Research Association of New Zealand,P.O.Box 8094,Palmerston North 4472,New Zealand [2]Australian Centre for Neutron Scattering,ANSTO,Lucas Heights,NSW 2234,Australia
出 处:《Journal of Leather Science and Engineering》2019年第1期114-122,共9页皮革科学与工程(英文)
基 金:financially supported by the Ministry of Business,Innovation and Employment(MBIE)through LASRA Strategic Science Investment Funding(SSIF).Grant Number LSRX1801.
摘 要:Collagen structure in biological tissues imparts its intrinsic physical properties by the formation of several covalent crosslinks.For the first time,two major crosslinks in the skin dihydroxylysinonorleucine(HLNL)and histidinohydroxymerodesmosine(HHMD),were isotopically labelled and then analysed by liquid-chromatography high-resolution accurate-mass mass spectrometry(LC-HRMS)and small-angle neutron scattering(SANS).The isotopic labelling followed by LC-HRMS confirmed the presence of one imino group in both HLNL and HHMD,making them more susceptible to degrade at low pH.The structural changes in collagen due to extreme changes in the pH and chrome tanning were highlighted by the SANS contrast variation between isotopic labelled and unlabelled crosslinks.This provided a better understanding of the interaction of natural crosslinks with the chromium sulphate in collagen suggesting that the development of a benign crosslinking method can help retain the intrinsic physical properties of the leather.This analytical method can also be applied to study artificial crosslinking in other collagenous tissues for biomedical applications.
关 键 词:CROSSLINKS Isotopic labelling LC-HRMS Quantitative analysis SANS Collagen structure
分 类 号:R74[医药卫生—神经病学与精神病学]
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