Stawikowski Maciej J, Fields Gregg B
Department of Chemistry and Biochemistry, Florida Atlantic University, 777 Glades Rd, Boca Raton, FL 33431.
The Scripps Research Institute/Scripps Florida, 130 Scripps Way, Jupiter, FL 33458.
Tetrahedron Lett. 2018 Jan 10;59(2):130-134. doi: 10.1016/j.tetlet.2017.12.008. Epub 2017 Dec 5.
A novel and convenient method for the synthesis of -terminally branched collagen-model peptides has been achieved using tricine (-[tris(hydroxymethyl)methyl]glycine) as a branching scaffold and 1,2-diaminoethane or 1,4-diaminobutane as a linker. The peptide sequence was incorporated directly onto the linker and scaffold during solid-phase synthesis without additional manipulations. The resulting branched triple-helical peptides exhibited comparable thermal stabilities to the parent, unbranched sequence, and served as substrates for matrix metalloproteinase-1 (MMP-1). The tricine-based branch reported herein represents the simplest synthetic scaffold for the convenient synthesis of covalently linked homomeric collagen-model triple-helical peptides.
使用三（羟甲基）甲基甘氨酸（tricine）作为分支支架，1,2-二氨基乙烷或1,4-二氨基丁烷作为连接体，已实现了一种新颖且便捷的合成C末端分支胶原模型肽的方法。在固相合成过程中，无需额外操作，肽序列直接整合到连接体和支架上。所得的分支三螺旋肽表现出与未分支的亲本序列相当的热稳定性，并作为基质金属蛋白酶-1（MMP-1）的底物。本文报道的基于tricine的分支代表了用于方便合成共价连接的同聚胶原模型三螺旋肽的最简单合成支架。
