A new 14 peptide, originating essentially from the helix 5 of HPV 16L1, illustrates an IC50 of 19.38 nM for the inhibition of HPV 16 L1 pentamer formation, which is highly efficient for targeting a specific protein segment. In addition, mechanism studies reveal that the length, sequence, and the folding of the peptide are critical factors for its inhibition. Particularly, the peptide shows similar inhibition against the pentamer formation of HPV 58L1, although it is designed specially for HPV 16 L1. This study opens a way for the development of high-efficiency, broad-spectrum inhibitors as a new class of anti-HPV agents, which could be extended to the treatment of other virus types.
基金：
NSFCNational Natural Science Foundation of China [21373101, 91027027, 20934002]; Innovation Program of State Key Laboratory for Supramolecular Structure and Materials
第一作者机构：[1]State Key Laboratory of Supramolecular Structure and Materials, Institute of Theoretical Chemistry, Jilin University, No. 2699, Qianjin Street, Changchun 130012, China
通讯作者：
推荐引用方式(GB/T 7714)：
Fu Ding-Yi,Jin Shi,Zheng Dong-Dong,et al.Peptidic Inhibitors for in Vitro Pentamer Formation of Human Papillomavirus Capsid Protein L1[J].ACS MEDICINAL CHEMISTRY LETTERS.2015,6(4):381-385.doi:10.1021/ml500392y.
APA：
Fu, Ding-Yi,Jin, Shi,Zheng, Dong-Dong,Zha, Xiao&Wu, Yuqing.(2015).Peptidic Inhibitors for in Vitro Pentamer Formation of Human Papillomavirus Capsid Protein L1.ACS MEDICINAL CHEMISTRY LETTERS,6,(4)
MLA：
Fu, Ding-Yi,et al."Peptidic Inhibitors for in Vitro Pentamer Formation of Human Papillomavirus Capsid Protein L1".ACS MEDICINAL CHEMISTRY LETTERS 6..4(2015):381-385
