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作 者:郑少东[1,2] 胡杨[1,2] 但年华[1,2] 但卫华[1,2] 琚海燕[1,2]
机构地区:[1]四川大学生物医学工程技术研究中心,四川成都610065 [2]四川大学皮革化学与工程教育部重点实验室,四川成都610065
出 处:《中国皮革》2014年第17期23-26,30,共5页China Leather
基 金:教育部博士点基金项目(20130181110092)
摘 要:六氟异丙醇(HFIP)通常作为制备I型胶原纳米纤维的溶剂,然而,其对I型胶原分子结构的影响还需全面的论证。以HFIP为溶剂,配制质量浓度为3%、5%、7%的I型胶原溶液,室温(约20℃)下搅拌3d,冷冻干燥制得准变性胶原(PDC)。采用凝胶电泳法、紫外光谱法、傅里叶红外光谱法、热重法、超灵敏差式扫描量热法和X射线衍射法,对PDC分子结构进行表征。结果显示:HFIP的2个三氟甲基有助于打破疏水作用的联系,HFIP的醇羟基有助于打断I型胶原的氢键,使其三股螺旋结构遭到破坏,分子间氢键作用减弱,形成了与明胶不同的多肽链聚集结构,HFIP中的酸性二级醇羟基降低了I型胶原的热变性温度,且热稳定性均降低。结果表明,HFIP可能不适合作为I型胶原的良溶剂。A series of solutions were prepared by dissolving type I Collagen in HFIP and the mass concentrations were 3%, 5% ,7% ,respectively. After stirred for 3 days at 20℃, the solutions were freeze - dried to gain prospective degeneration collagen (PDC). The molecular structure of PDC was characterized by SDS - PAGE, UV, FF - IR, TG, US - DSC and XRD. The results show that the two trifluoromethyl groups of HFIP contribute to break the hydrophobic interactions, the alcohol hydroxyl of HFIP contributes to break the hydrogen bonds of type I collagen, then the triple - helical structure of type I collagen is destroyed and in- termolecular hydrogen bonding is weakened. The type I collagen forms an polypeptide chain structure which is different from gelati-n, and the denature temperature of collagen is decreased by the acidic secondary alcohol hydroxyl of HFIP lead to reduction of the thermal stability. It can be concluded that HFIP is not the suitable solvent for type I collagen.
分 类 号:TS51[轻工技术与工程—皮革化学与工程]
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