四羟甲基季鏻盐与胶原蛋白的结合

Combination of Tetrakis Hydroxymethyl Phosphonium Chloride with Collagen Protein

用白皮粉作为胶原蛋白模拟物与四羟甲基氯化(THPC)反应,研究了THPC与胶原蛋白的反应特点。通过研究THPC与聚己内酰胺、聚乙烯醇、乙二胺的酰胺基、羟基、氨基的反应,间接证明THPC主要与胶原蛋白的氨基结合,可与氨基以n(P)∶n(N)=1.0∶2.2形成交联,THPC与羟基和酰胺基均有少量结合,并在pH=8.0时结合量最高。通过31P NMR分析表明,三羟甲基氧化膦(THPO)与氨基没有反应活性,与胶原蛋白结合的结构形式主要是四羟甲基氢氧化(THPOH)或三羟甲基膦(THP)。

To understand the reaction of tetrakis hydroxymethyl phosphonium chloride （THPC） with collagen protein, the interactions of THPC with polycaprolactam, poly vinyl alcohol or ethylenediamine which were used as the model substances of amido, hydroxy and amino groups of collagen protein were examed. It was found that tetrakis hydroxymethyl phosphonium mainly linked with amino groups of collagen, while less with hydroxy groups or amido groups at a mole ratio of n （P） ： n （N） = 1 ： 2. 2. The combination capacities of tetrakis hydroxymethyl phosphonium chloride with hydroxy groups and amido groups changed with pH, it reached the maximum at pH = 8.0. The ^31P NMR spectra indicate that trihydroxymethyl phosphonium hydroxide（THPOH） or trihydroxymethyl phosphine（THP） was an effective crosslinking agent and THPO was not reactive to collagen protein.