Design of coiled-coil N-peptides against HIV-1 based on a CADD strategy

Org Biomol Chem. 2024 Dec 18;23(1):157-166. doi: 10.1039/d4ob01620c.

Abstract

Human Immunodeficiency Virus (HIV) has continued to endanger human health for decades and has a substantial impact on global health defence. Peptide-based fusion inhibitors, as an integral part of Highly Active Anti-Retroviral Therapy (HAART), are effective in preventing and controlling the AIDS epidemic. Nevertheless, the current market leader, Enfuvirtide, is facing numerous challenges in clinical application. We herein devised a cutting-edge development strategy leveraging SWISS-MODEL and HDOCK, enabling the design of artificial N-peptides. The most active compound, IZNP02QE, surpassed the positive control by demonstrating remarkable nanomolar-level inhibitory activity against HIV-1. Mechanistic investigations unveiled IZNP02QE's ability to disrupt the crucial endogenous 6-helix bundle (6-HB) by forming heteropolymers, underscoring its potential as a novel anti-HIV-1 agent. This work not only pioneers a novel design methodology for N-peptides but also opens up the possibility of a CADD strategy for designing peptide-based fusion inhibitors.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Anti-HIV Agents / chemical synthesis
  • Anti-HIV Agents / chemistry
  • Anti-HIV Agents / pharmacology
  • Drug Design*
  • HIV-1* / drug effects
  • Humans
  • Models, Molecular
  • Peptides* / chemical synthesis
  • Peptides* / chemistry
  • Peptides* / pharmacology

Substances

  • Peptides
  • Anti-HIV Agents