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ACS medicinal chemistry letters
Apr 09, 2015;6 (4): 381-5.

Peptidic inhibitors for in vitro pentamer formation of human papillomavirus capsid protein l1.

Ding-Yi Fu, Shi Jin, Dong-Dong Zheng, Xiao Zha, Yuqing Wu
Author Information
  1. Ding-Yi Fu: State Key Laboratory of Supramolecular Structure and Materials, Institute of Theoretical Chemistry, Jilin University , No. 2699, Qianjin Street, Changchun 130012, China.
  2. Shi Jin: State Key Laboratory of Supramolecular Structure and Materials, Institute of Theoretical Chemistry, Jilin University , No. 2699, Qianjin Street, Changchun 130012, China.
  3. Dong-Dong Zheng: State Key Laboratory of Supramolecular Structure and Materials, Institute of Theoretical Chemistry, Jilin University , No. 2699, Qianjin Street, Changchun 130012, China.
  4. Xiao Zha: Sichuan Tumor Hospital & Institute , Chengdu 610041, China.
  5. Yuqing Wu: State Key Laboratory of Supramolecular Structure and Materials, Institute of Theoretical Chemistry, Jilin University , No. 2699, Qianjin Street, Changchun 130012, China.
PMID: 25893037 DOI: 10.1021/ml500392y

Abstract

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.

Keywords

Peptide human papillomavirus inhibitor pentamer formation

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