Marastoni M, Salvadori S, Balboni G, Spisani S, Gavioli R, Traniello S, Tomatis R
Department of Pharmaceutical Sciences, University of Ferrara, Italy.
Arzneimittelforschung. 1989 Aug;39(8):926-8.
Fifteen pentapeptide analogs of C-terminal fragment of peptide T, H-Ala-Ser-Thr-Thr-Thr-Asn-Tyr-Thr-OH, were prepared and tested for human monocyte chemotaxis. Structure-activity studies suggest that the potent chemotactic activity of H-Thr-Thr-Asn-Tyr-Thr-OH is mediated through the polar properties of the C-terminal carboxyl group and Thr side chains at the critical positions 5 and 8, while the hydroxyl group of N-terminal Thr and its free amino function are not essential requirements for CD4 receptor interactions.
制备了十五种肽T C末端片段H-Ala-Ser-Thr-Thr-Thr-Asn-Tyr-Thr-OH的五肽类似物，并对其进行了人单核细胞趋化性测试。构效关系研究表明，H-Thr-Thr-Asn-Tyr-Thr-OH的强趋化活性是通过C末端羧基以及关键位置5和8处苏氨酸侧链的极性特性介导的，而N末端苏氨酸的羟基及其游离氨基功能并非CD4受体相互作用的必要条件。
