Characterization of Acid-Soluble Type I Collagen in Solution by Viscosity Measurements. I. Some evidence about adsorption on the glass material and about electrostatic and ionic bondings in the molecular self assembly process

Jean-Claude Ronzon
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引用次数: 2

Abstract

The evidence of a adsorption phenomenon of the acid-soluble collagen molecules on the glass material is shown. A way of calculation is proposed from viscosimetric measurements. It could be pointed out that a small amount corresponding to 4 to 5% of the collagenous concentration is involved in such a adsorption process, at 25 °C. This adsorption phenomenon is temperature-dependent and weakened by a previous NaOH-treatment of the collagen solutions.

It is confirmed that intermolecular associations may take place in acidic conditions and they are minimized for a pH range corresponding to the pK area of aspartic and glutamic acid residues. The influence of temperature showed that ionic interactions are reinforced by hydrophobic effects. The modification of the ionization and the removal of the telopeptidic regions from the native molecules are responsible for the decrease in these associations. On the other hand, it was shown that the relative flexibility of the molecule may explain the modifications in the {η} values depending on the pH and ionic-strength conditions for the molecular solutions.

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酸溶型I型胶原在溶液中的粘度测定。1 .关于在玻璃材料上的吸附和分子自组装过程中的静电和离子键的一些证据
证明了酸溶性胶原蛋白分子在玻璃材料上的吸附现象。提出了一种从粘度测量出发的计算方法。可以指出的是,在25℃下,这种吸附过程只涉及到相当于胶原浓度4 - 5%的少量。这种吸附现象是温度依赖性的,并通过先前的naoh处理胶原蛋白溶液而减弱。研究证实,在酸性条件下可能发生分子间结合,并且在与天冬氨酸和谷氨酸残基的pK面积相对应的pH范围内,分子间结合最小。温度的影响表明,疏水效应增强了离子相互作用。电离的修饰和从天然分子中去除末端肽区是导致这些关联减少的原因。另一方面,表明分子的相对柔韧性可以解释{η}值的变化取决于分子溶液的pH和离子强度条件。
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