Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
August 19, 2010
VIP: The Active Core in a Triazole Peptide Dual-Site Antagonist of HIV-1 gp120
Muddegowda Umashankara, Karyn McFadden, Isaac Zentner, Arne Schön, Srivats Rajagopal, Ferit Tuzer, Syna A. Kuriakose, Mark Contarino, Judith LaLonde, Ernesto Freire, and Irwin Chaiken*
Chaiken and colleagues describe their work in minimizing the structural complexity of a lead class of peptide triazole inhibitors of the HIV-1 envelope protein gp120. By using a combination of chemical synthesis, molecular binding analysis, and antiviral cell infection assays, they identified HIV-1 cell entry inhibitor leads that can be used as tools to develop therapeutic and microbicidal agents for AIDS treatment and prevention. These results help to define the pharmacophore that enables dual antagonism of the envelope protein and to improve opportunities for peptidomimetic design of advanced HIV-1 inhibitor leads.
This work by Chaiken and co-workers will be part of an upcoming special issue of ChemMedChem that will contain a core series of research articles published in recognition of the past quarter century of anti-HIV drug discovery and development.
Received May 21, 2010; published online August 2, 2010, DOI: 10.1002/cmdc.201000222.