Khasanova Tatyana V, Khakshoor Omid, Nowick James S
Department of Chemistry, University of California, Irvine, Irvine, California 92697-2025, USA.
Org Lett. 2008 Nov 20;10(22):5293-6. doi: 10.1021/ol8021897. Epub 2008 Oct 21.
This paper introduces polar and hydrophobic variants of the unnatural amino acid Hao, which mimics the hydrogen-bonding functionality of one edge of a beta-strand. In these variants, the methyl side chain of Hao is replaced with acidic, basic, and hydrophobic groups. These modifications can impart improved solubility and additional side-chain interactions to peptides containing Hao.
本文介绍了非天然氨基酸Hao的极性和疏水性变体,该变体模拟了β-链一侧边缘的氢键功能。在这些变体中,Hao的甲基侧链被酸性、碱性和疏水性基团取代。这些修饰可以提高含Hao肽的溶解度,并增加其侧链相互作用。