Abstract
We present a new approach for the covalent inhibition of HIV-1 integrase (IN) by an LEDGF/p75-derived peptide modified with an N-terminal succinimide group. The covalent inhibition is mediated by direct binding of the succinimide to the amine group of a lysine residue in IN. The peptide serves as a specific recognition sequence for the target protein, while the succinimide serves as the binding moiety. The combination of a readily synthesizable peptide precursor with easy and efficient binding to the target protein makes this approach a promising new strategy for designing lead compounds.
| Original language | English |
|---|---|
| Pages (from-to) | 1987-1994 |
| Number of pages | 8 |
| Journal | ChemMedChem |
| DOIs | |
| State | Published - 2016 |
Bibliographical note
Publisher Copyright:© 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
UN SDGs
This output contributes to the following UN Sustainable Development Goals (SDGs)
-
SDG 3 Good Health and Well-being
Keywords
- HIV-1 integrase
- covalent inhibitors
- peptides
- succinimide
Fingerprint
Dive into the research topics of 'Covalent Inhibition of HIV-1 Integrase by N-Succinimidyl Peptides'. Together they form a unique fingerprint.Cite this
- APA
- Author
- BIBTEX
- Harvard
- Standard
- RIS
- Vancouver