Department of Pharmaceutical Health Care, Faculty of Pharmaceutical Sciences, Himeji Dokkyo University, Hyogo, Japan.
J Pept Sci. 2010 Apr;16(4):165-70. doi: 10.1002/psc.1215.
The synthetic peptide fragment (LC5: LRCRNEKKRHRAVRLIFTI) inhibits human immunodeficiency virus type 1 (HIV-1) infection of MT-4 cells. In this study, the solution structure of LC5 in SDS micelles was elucidated by using the standard (1)H two-dimensional NMR spectroscopic method along with circular dichroism and fluorescence quenching. The peptide adopts a helical structure in the C-terminal region (residues 13-16), whereas the N-terminal part remains unstructured. The importance of Phe17 in maintaining the structure of LC5 was demonstrated by replacing Phe17 with Ala, which resulted in the dramatic conformational change of LC5. The solution structure of LC5 elucidated in the present work provides a basis for further study of the mechanism of the inhibition of HIV-1 infection.
合成肽片段 (LC5: LRCRNEKKRHRAVRLIFTI) 可抑制人类免疫缺陷病毒 1 型 (HIV-1) 对 MT-4 细胞的感染。在这项研究中，使用标准的 (1)H 二维 NMR 波谱学方法以及圆二色性和荧光猝灭法，阐明了 LC5 在 SDS 胶束中的溶液结构。该肽在 C 末端区域（残基 13-16）呈螺旋结构，而 N 端部分仍未形成结构。通过用丙氨酸替换苯丙氨酸 17 来证明苯丙氨酸 17 对维持 LC5 结构的重要性，这导致 LC5 的构象发生了显著变化。本工作阐明的 LC5 的溶液结构为进一步研究抑制 HIV-1 感染的机制提供了基础。
