Fields Gregg B
Department of Chemistry and Biochemistry, Florida Atlantic University, Jupiter, FL, USA.
Department of Chemistry, Scripps Research, Jupiter, FL, USA.
Methods Mol Biol. 2019;1944:229-252. doi: 10.1007/978-1-4939-9095-5_17.
The triple-helical structure of collagen has been accurately reproduced in numerous chemical and recombinant model systems. Triple-helical peptides have found application for dissecting collagen-stabilizing forces, isolating receptor and protein binding sites in collagen, evaluating collagen-mediated cell signaling activities, mechanistic examination of collagenolytic proteases, and developing novel biomaterials and drug delivery vehicles. Due to their inherent stability to general proteolysis, triple-helical peptides present an opportunity as in vivo inhibitory agents. The present chapter provides methods for the construction of collagen-based triple-helical peptides designed as matrix metalloproteinase inhibitors.
胶原蛋白的三螺旋结构已在众多化学和重组模型系统中得到精确再现。三螺旋肽已被应用于剖析胶原蛋白稳定力、分离胶原蛋白中的受体和蛋白质结合位点、评估胶原蛋白介导的细胞信号传导活性、对胶原蛋白水解蛋白酶进行机制研究,以及开发新型生物材料和药物递送载体。由于其对一般蛋白水解具有固有的稳定性,三螺旋肽提供了作为体内抑制剂的机会。本章提供了设计为基质金属蛋白酶抑制剂的基于胶原蛋白的三螺旋肽的构建方法。