Synthesis and conformational analysis of cyclotetrapeptide mimetic beta-turn templates and validation as 3D scaffolds.
The conformations of all stereoisomers of PMRI cyclotetrapeptide mimetics 1-8 are essentially determined by the predisposition of the diamine to stabilize beta-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 alpha(v)beta(3)-integrin receptor antagonists.
Gentilucci
Luca
L
Department of Chemistry "G. Ciamician", University of Bologna, Italy. gentilucci@unibo.it
Cardillo
Giuliana
G
Tolomelli
Alessandra
A
De Marco
Rossella
R
Garelli
Andrea
A
Spampinato
Santi
S
Spartà
Antonino
A
Juaristi
Eusebio
E
D040761:Biomimetic Materials / Q000737:chemistry* / Q000494:pharmacology*; D002448:Cell Adhesion / Q000187:drug effects; D002460:Cell Line; D045744:Cell Line, Tumor; D003198:Computer Simulation; D006801:Humans; D021621:Imaging, Three-Dimensional / Q000379:methods*; D039302:Integrin alphaVbeta3 / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008968:Molecular Conformation; D010456:Peptides, Cyclic / Q000737:chemistry*
D039302:Integrin alphaVbeta3; D010456:Peptides, Cyclic