Ojida Akio, Miyahara Yoshifumi, Kohira Takahiro, Hamachi Itaru
Department of Chemistry and Biochemistry, Graduate School of Engineering, Kyushu University, Fukuoka 812-8581, Japan.
Biopolymers. 2004;76(2):177-84. doi: 10.1002/bip.10574.
Many biological processes are mediated by surface recognition between proteins. Small molecules that recognize and bind a specific region of a protein surface may be promising agents for disrupting certain protein-protein surface interactions, which consequently leads to regulation of cellar functions. This article describes our recent efforts toward the development of the designed small molecules, which can recognize histidine or phosphorylated amino acid residues on peptide surfaces in a sequence-selective manner. These results demonstrate that cooperative metal-ligand interaction is powerful for tight and selective binding to the specific amino acid residues of proteins in aqueous medium.
许多生物过程是由蛋白质之间的表面识别介导的。能够识别并结合蛋白质表面特定区域的小分子可能是破坏某些蛋白质-蛋白质表面相互作用的有前景的试剂，进而导致细胞功能的调节。本文描述了我们近期在设计小分子方面所做的努力，这些小分子能够以序列选择性的方式识别肽表面的组氨酸或磷酸化氨基酸残基。这些结果表明，在水性介质中，金属-配体协同相互作用对于紧密且选择性地结合蛋白质的特定氨基酸残基具有强大作用。
