Degree of crosslinking of collagen at interfaces: Adhesion and shear rheological indicators
Degree of crosslinking of collagen at interfaces: Adhesion and shear rheological indicators
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DOI：
10.1016/j.ijbiomac.2010.09.017
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发表时间：
2011-01-01
影响因子：
8.2
通讯作者：
Miller, R.
中科院分区：
文献类型：
--
作者：
Fathima, N. Nishad;Dhathathreyan, Aruna;Miller, R.
以固/气和液/气界面的粘附功和表面流变学为指标，研究了碱性硫酸铬(BCS)、单宁酸、儿茶素和甲醛等交联剂对胶原蛋白的稳定作用。结果表明，6，W的增加对吸附有促进作用，而对吸附有阻碍作用。对胶原蛋白的剪切流变学研究表明，随着时间的推移，剪切粘度和弹性都会增加，而对于含有儿茶素和单宁酸等多酚的胶原蛋白，这些值都有不寻常的下降。流变性和粘附功之间的相关性表明，不同交联剂的胶原蛋白开始粘弹性行为的时间框架决定了蛋白质的最终宏观性质。这项研究试图通过水合蛋白质和交联剂组装过程中水分子的动力学和强度来量化胶原的交联度。(C)2010爱思唯尔B.V.保留所有权利。
Work of adhesion (Delta W) and surface rheology at solid/air and solution/air interface have been used as indicators to study the stabilization of collagen by different crosslinking agents like basic chromium sulfate (BCS), tannic acid, catechin and formaldehyde. The results show that an increase in rate of 6,W would promote adsorption while a decrease leads to hindered adsorption. Shear rheological studies on collagen demonstrate an increase in both shear viscosity and elasticity with time while for collagen with polyphenols like catechin and tannic acid there is an unusual breakdown of these values. A correlation between the rheological properties and the work of adhesion suggests that the time frame in which the viscoelastic behavior is initiated for collagen with different crosslinking agents determines the final macroscopic property of the protein. The study attempts to quantify the degree of crosslinking of collagen through the dynamics and strength of the water molecules in the assembly of hydrated protein and the crosslinking agents. (C) 2010 Elsevier B.V. All rights reserved.