Center for Biologically Inspired Systems Science, Indian Institute of Technology Jodhpur, Old Residency Road, Jodhpur 342011, Rajasthan, India.
Biochem Biophys Res Commun. 2014 Jun 13;448(4):480-4. doi: 10.1016/j.bbrc.2014.04.135. Epub 2014 May 4.
Both collagen and amyloidogenic proteins have an inherent ability to undergo a self-assembly process leading to formation of supramolecular structures. Though our understanding of collagen-amyloid link is very poor, a few experimental evidences have indicated the protective nature of collagen against amyloid fibril formation. To further our understanding of collagen-amyloid relationship, we have explored the role of type I collagen on amyloid-aggregation of lysozyme. Thioflavin-T assay data indicated strong inhibition of both spontaneous and seeded aggregation of lysozyme by collagen. Both chemical and thermal denaturation experiments have showed increased lysozyme stability in the presence of collagen. However, the presence of collagen did not alter lysozyme activity. These findings confirm that type I collagen is capable of blocking or interfering with the amyloid aggregation of lysozyme, and the results may have significant implications for the design of collagen based therapeutics against aggregation of disease linked amyloidogenic proteins.
胶原蛋白和淀粉样蛋白都具有内在的自组装能力，导致超分子结构的形成。尽管我们对胶原蛋白-淀粉样蛋白的联系了解甚少，但一些实验证据表明胶原蛋白对淀粉样纤维形成具有保护作用。为了进一步了解胶原蛋白-淀粉样蛋白的关系，我们研究了Ⅰ型胶原蛋白对溶菌酶淀粉样聚集的作用。噻唑蓝-T 检测数据表明胶原蛋白强烈抑制溶菌酶的自发和接种聚集。化学和热变性实验均表明胶原蛋白存在时溶菌酶稳定性增加。然而，胶原蛋白的存在并不改变溶菌酶的活性。这些发现证实，Ⅰ型胶原蛋白能够阻止或干扰溶菌酶的淀粉样聚集，并且该结果可能对基于胶原蛋白的治疗剂的设计具有重要意义，以防止与疾病相关的淀粉样蛋白聚集。
