Restricting the flexibility of crosslinked, interfacial peptide inhibitors of HIV-1 protease

L G Ulysse; J Chmielewski

doi:10.1016/s0960-894x(98)00595-2

Restricting the flexibility of crosslinked, interfacial peptide inhibitors of HIV-1 protease

Bioorg Med Chem Lett. 1998 Nov 17;8(22):3281-6. doi: 10.1016/s0960-894x(98)00595-2.

Authors

L G Ulysse¹, J Chmielewski

Affiliation

¹ Department of Chemistry, Purdue University, West Lafayette, IN 47907, USA.

PMID: 9873718
DOI: 10.1016/s0960-894x(98)00595-2

Abstract

Interfacial peptides of HIV-1 protease were crosslinked with varying length alkyl-chains containing either a single cis or trans double bond, or a triple bond to remove degrees of freedom within the tethers. The synthesis of these compounds and their effects on the activity of HIV-1 protease are described.

Publication types

Research Support, U.S. Gov't, P.H.S.

MeSH terms

HIV Protease / chemistry
HIV Protease / drug effects*
HIV Protease Inhibitors / chemical synthesis*
HIV Protease Inhibitors / pharmacology
Peptides / chemical synthesis*
Peptides / pharmacology
Structure-Activity Relationship

Substances

HIV Protease Inhibitors
Peptides
HIV Protease

Grants and funding

R01 GM52739/GM/NIGMS NIH HHS/United States