Linear and cyclic glycopeptide as HIV protease inhibitors.

Sachin A Pawar, Amit M Jabgunde, Glenn E M Maguire, Hendrik G Kruger, Yasien Sayed, Mahmoud E S Soliman, Dilip D Dhavale, Thavendran Govender

Journal: European journal of medicinal chemistry 2013;60():144-54

PMID: 23291117

Full Text on Elsevier Science View on PubMed

Abstract

Novel linear and cyclic glycotetrapeptides were designed, synthesized and tested for inhibition of the wild type C-SA HIV-1 protease enzyme. The incorporation of β-amino acid sugar to the linear and cyclic peptides resulted in a series of fifteen novel compounds. Linear glycopeptide 4a and cyclic glycopeptide 6a displayed significant activities against the HIV protease enzyme. The experimental results were compared with a computational approach using molecular docking. The sugar hydroxyl group at the C(3) position in linear (4a) as well as cyclic glycopeptide (6a), shows hydrogen bonding interaction with the enzymatic Asp25/Asp25' residues in docking studies.

Address: Catalysis and Peptide Research Unit, School of Health Sciences, University of KwaZulu-Natal, South Africa.

DOI: 10.1016/j.ejmech.2012.11.018

Link outs

Free resources

Other Literature Sources:

Miscellaneous:

https://assays.cancer.gov/non-CPTAC-1105

Subscription / membership required

Full Text Sources:

https://linkinghub.elsevier.com/retrieve/pii/S0223...

MeSH Terms: Dose-Response Relationship, Drug, Glycopeptides, HIV Protease, HIV Protease Inhibitors, Models, Molecular, Molecular Structure, Structure-Activity Relationship