2019,
Journal of Leather Science and Engineering.
DOI:
10.1186/s42825-019-0012-x
Quantitative and structural analysis of isotopically labelled natural crosslinks in type I skin collagen using LC-HRMS and SANS
Yi Zhang, Rafea Naffa, Christopher J. Garvey, Catherine A. Maidment, Sujay Prabakar
Abstract:
Abstract
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.
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2024-04-28 18:09:00
李翛然:
#paper doi:10. 1186/s42825-019-0012-x Nature Communication. Quantitative and structural analysis of isotopically labelled natural crosslinks in type I skin collagen using LC-HRMS and SANS 本文介绍了对使用LC-HRMS和SANS对标记同位素的天然交联物在I型皮肤胶原蛋白中进行定量和结构分析的研究。研究重点放在皮肤中的两种主要交联物HLNL和HHMD上，它们被同位素标记并进行分析，以了解它们的结构变化以及与硫酸铬的相互作用。研究强调了开发一种良性交联方法的重要性，以保留胶原蛋白的固有物理特性，特别是在皮革制造行业。主要发现包括确认HLNL和HHMD中各有一个亚胺基，使它们容易在低pH值下降解，并由于极端pH值变化和铬鞣制造导致胶原蛋白的结构变化。本研究使用的分析方法也可应用于研究其他胶原组织中的人工交联，用于生物医学应用。 这个算是人类第一篇弄清楚了胶原蛋白到底有哪些交联键~~所以化学交联的方法基本没戏，还是生物方法吧。~