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Cover Picture: Covalent Inhibition of HIV‐1 Integrase by N ‐Succinimidyl Peptides (ChemMedChem 18/2016)
Author(s) -
Chandra Koushik,
Das Priyadip,
Mamidi Samarasimhareddy,
Hurevich Mattan,
IosubAmir Anat,
Metanis Norman,
Reches Meital,
Friedler Assaf
Publication year - 2016
Publication title -
chemmedchem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 0.817
H-Index - 100
eISSN - 1860-7187
pISSN - 1860-7179
DOI - 10.1002/cmdc.201600435
Subject(s) - succinimide , integrase , chemistry , moiety , peptide , covalent bond , residue (chemistry) , stereochemistry , combinatorial chemistry , biochemistry , dna , organic chemistry
The front cover picture shows the covalent inhibition of HIV‐1 Integrase (IN) (blue) by a lens epithelium‐derived growth factor (LEDGF/p75)‐derived peptide modified with N ‐terminal succinimide (yellow). The covalent inhibition is mediated by direct binding of the succinimide to the amine group of a lysine residue in IN, indicated by the red lock. The peptide serves as a specific recognition sequence for the target protein, while the succinimide serves as the binding moiety. The combination of an easy‐to‐synthesize peptide precursor with easy and efficient binding to the target protein makes this approach a promising new strategy for designing lead compounds. More information can be found in the Full Paper by Assaf Friedler et al. on page 1987 in Issue 18, 2016 (DOI: 10.1002/cmdc.201600190).