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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)。
Using white powder as collagen analogue and tetramethylol chloride (THPC) reaction, the reaction between THPC and collagen was studied. By studying THPC reaction with polycaprolactam, polyvinylalcohol, ethylenediamine amido, hydroxyl and amino, THPC indirectly proves that THPC mainly binds to the amino group of collagen and can react with amino group at n (P): n (N) = 1.0 : 2.2 The formation of cross-linked, THPC with hydroxyl and amide groups have a small amount of binding, and when pH = 8.0, the highest amount of binding. 31P NMR analysis showed that trihydroxymethylphosphine oxide (THPO) had no reactivity with amino groups, and the primary structure of collagen binding was THPOH or THP.