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The Constrained Amino Acid β‐Acc Confers Potency and Selectivity to Integrin Ligands
Author(s) -
Urman Sylwia,
Gaus Katharina,
Yang Yi,
Strijowski Ulf,
Sewald Norbert,
De Pol Silvia,
Reiser Oliver
Publication year - 2007
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.200605248
Subject(s) - integrin , vitronectin , chemistry , peptide , enantiomer , block (permutation group theory) , selectivity , potency , ic50 , amino acid , biochemistry , combinatorial chemistry , stereochemistry , cell , computational biology , biology , mathematics , combinatorics , in vitro , catalysis
Complete opposites: The incorporation of the rigid building block (+)‐β‐Acc (Acc=aminocyclopropane carboxylic acid) into cyclic RGD peptides results in a high affinity towards the integrin α v β 3 . The peptides 1 and 2 are composed of the enantiomeric building blocks (+)‐ (blue) and (−)‐β‐Acc (red). The active peptide 1 inhibits integrin α v β 3 mediated cell adhesion to vitronectin with an IC 50 value of 20 n M .
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