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A Conformationally Frozen Peptoid Boosts CXCR4 Affinity and Anti‐HIV Activity
Author(s) -
Demmer Oliver,
Frank Andreas O.,
Hagn Franz,
Schottelius Margret,
Marinelli Luciana,
Cosconati Sandro,
BrackWerner Ruth,
Kremb Stephan,
Wester HansJürgen,
Kessler Horst
Publication year - 2012
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201202090
Subject(s) - peptoid , pentapeptide repeat , human immunodeficiency virus (hiv) , nitrogen atom , homogeneous , chemistry , peptide , cxcr4 , stereochemistry , computational biology , combinatorial chemistry , biochemistry , receptor , chemokine , biology , virology , mathematics , combinatorics , organic chemistry , group (periodic table)
There can be only one : Using a peptoid motif obtained by shifting the arginine side chain of a pentapeptide previously developed by Fujii et al. to the neighboring nitrogen atom restricts the conformational freedom and yields a conformationally homogeneous peptide (see picture) with a 100‐fold higher binding affinity to the chemokine receptor CXCR4 in the picomolar range. Its efficiency to inhibit HIV‐1 infections is also demonstrated.