Suppr超能文献

[胶原蛋白矿化中晶核位点的研究]

[Study of the nucleation sites in collagen mineralization].

作者信息

Huang Zhao-long, Zhang Wei, Cui Fu-zhai

机构信息

Department of Materials Science and Engineering, Tsinghua University, Beijing 100084, China.

出版信息

Guang Pu Xue Yu Guang Pu Fen Xi. 2004 May;24(5):539-42.

Abstract

By comparing IR spectra of collagen, collagen/CaCl2 and collagen/calcium phosphate, it was found that intensities of amide I, II and III bands were significantly decreased after mineralization. Band amide I shifted to wards lower wave number. This shift indicated chemical interaction between carboxyl groups and Ca ions formed in the mineralization. The result indicated that there was another nucleation site, i.e. carbonyl [structure: see text] on collagen, besides the previous reported nucleation site of carboxyl (-COOH) on collagen. The decrease of amide I peak intensity was mainly due to blockage of C=O stretch. Comparing the IR spectra of demineralized collagen and pure collagen, amide I, II and III peaks intensity and position were almost the same. When the mineral dissolved, amide peaks rebounded, which indicated that the crystals nucleated on these sites enwrapped the groups and blocked the groups vibration. The decreases of peak intensity of amide I, II and III were different due to their different vibration modes. The result confirmed that the carbonyl group was one kind of the nucleation site during collagen mineralization. The relationship between the process of collagen mineralization and variety of amide bonds was also studied.

摘要

通过比较胶原蛋白、胶原蛋白/CaCl₂和胶原蛋白/磷酸钙的红外光谱,发现矿化后酰胺I、II和III带的强度显著降低。酰胺I带向更低波数移动。这种移动表明矿化过程中羧基与钙离子之间形成了化学相互作用。结果表明,除了先前报道的胶原蛋白上的羧基(-COOH)成核位点外,胶原蛋白上还存在另一个成核位点,即羰基[结构:见原文]。酰胺I峰强度的降低主要是由于C=O伸缩受阻。比较脱矿化胶原蛋白和纯胶原蛋白的红外光谱,酰胺I、II和III峰的强度和位置几乎相同。当矿物质溶解时,酰胺峰反弹,这表明在这些位点成核的晶体包裹了基团并阻碍了基团振动。由于酰胺I、II和III的振动模式不同,它们峰强度的降低也不同。结果证实羰基是胶原蛋白矿化过程中的一种成核位点。还研究了胶原蛋白矿化过程与酰胺键变化之间的关系。

文献AI研究员

20分钟写一篇综述,助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型,支持多种主流文档格式。

立即体验