当前共找到 2 篇文献分享。
1.
李翛然
(2024-04-28 18:09):
#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。~
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) …
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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. Graphical abstract
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2.
李翛然
(2024-01-30 16:22):
#paper: doi:doi.org/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 这篇文章主要介绍了使用液相色谱-高分辨质谱（LC-HRMS）和小角散射（SANS）技术对I型皮肤胶原蛋白中的同位素标记天然交联物进行定量和结构分析的方法和结果。这项研究对于了解皮肤胶原蛋白的结构和功能具有重要意义。
1. 样品制备：研究使用了同位素标记的I型皮肤胶原蛋白样品，通过特定的实验方法进行制备。
2. 液相色谱-高分辨质谱（LC-HRMS）分析：研究使用LC-HRMS技术对样品中的同位素标记天然交联物进行定量分析。LC-HRMS技术能够提供高分辨率和高灵敏度的分析结果。
3. 小角散射（SANS）分析：研究使用SANS技术对样品中的同位素标记天然交联物进行结构分析。SANS技术能够提供关于样品中交联物的大小、形状和分布等信息。
这篇论文的优势包括：
1. 综合分析方法：研究采用了LC-HRMS和SANS两种不同的分析技术，能够从定量和结构两个方面全面地研究同位素标记天然交联物。
2. 高分辨率和高灵敏度：LC-HRMS技术具有高分辨率和高灵敏度的特点，能够提供准确的定量分析结果。
3. 结构信息获取：SANS技术能够提供关于交联物的结构信息，有助于深入了解其在皮肤胶原蛋白中的分布和作用。
然而，这篇论文也存在一些局限性：
1. 样品限制：研究中使用的是同位素标记的I型皮肤胶原蛋白样品，可能无法完全代表自然状态下的胶原蛋白。
2. 技术限制：虽然LC-HRMS和SANS技术在分析同位素标记天然交联物方面具有优势，但仍然存在一定的局限性，如分析时间较长、设备成本较高等。
3. 结果解释：由于同位素标记天然交联物的复杂性，对于分析结果的解释可能存在一定的挑战，需要进一步的研究和验证。
总体而言，这篇论文通过综合应用LC-HRMS和SANS技术，提供了一种定量和结构分析同位素标记天然交联物的方法，并揭示了其在I型皮肤胶原蛋白中的特征和作用，为进一步研究皮肤胶原蛋白的结构和功能提供了重要的参考。 这文章证是我的研究方向，帮助很大
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) …
>>>
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. Graphical abstract
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