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Synthesis and Conformational Analysis of Cyclotetrapeptide Mimetic β‐Turn Templates and Validation as 3D Scaffolds
Author(s) -
Gentilucci Luca,
Cardillo Giuliana,
Tolomelli Alessandra,
De Marco Rossella,
Garelli Andrea,
Spampinato Santi,
Spartà Antonino,
Juaristi Eusebio
Publication year - 2009
Publication title -
chemmedchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.817
H-Index - 100
eISSN - 1860-7187
pISSN - 1860-7179
DOI - 10.1002/cmdc.200800407
Subject(s) - pharmacophore , turn (biochemistry) , chemistry , template , combinatorial chemistry , peptide , integrin , molecule , molecular model , computational biology , stereochemistry , receptor , nanotechnology , biochemistry , biology , materials science , organic chemistry
The conformations of all stereoisomers of PMRI cyclotetrapeptide mimetics 1 – 8 are essentially determined by the predisposition of the diamine to stabilize β‐turns. The peptide mimetics can be regarded as 3D scaffolds for designing molecules with a predictable display of the pharmacophores. We used the models for testing novel RGD analogues as α v β 3 ‐integrin receptor antagonists.
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