Institute of Biostructures and Bioimaging, National Research Council , 80134 Naples, Italy , and Department of Chemistry and Biochemistry, University of Colorado , Boulder, Colorado 80309, United States.
Org Lett. 2013 Oct 18;15(20):5354-7. doi: 10.1021/ol402637d. Epub 2013 Oct 3.
A chemoselective, convenient, and mild synthetic strategy to modify peptides on a cysteine sulfhydryl group is described. It simply requires activated molecular sieves to selectively promote S-alkylation in the presence of peptide nucleophilic functionalities. The procedure is easy to perform, fast, and provides high yields even in the case of poor electrophilic groups. Moreover, the method allows an efficient one-pot poly alkylation, proving that the sulfhydryl reactivity does not rely on its specific position within the peptide sequence.
描述了一种在半胱氨酸巯基上修饰肽的化学选择性、方便和温和的合成策略。它只需使用活化分子筛即可在肽亲核性官能团存在下选择性促进 S-烷基化。该过程易于操作、快速，即使在亲电基团较差的情况下也能提供高产率。此外，该方法还允许有效的一锅多烷基化，证明巯基反应性不依赖于其在肽序列中的特定位置。
