Synthesis and biological evaluation of type VI beta-turn templated RGD peptidomimetics.
We report the design, synthesis, and binding affinities of a family of cyclic RGD peptides attached to type VI beta-turn scaffolds. The analogues prepared exhibit interesting binding data to the isolated receptors alphavbeta3 and alphavbeta5. The results demonstrate the utility of these type VI beta-turn scaffolds for the constraint of biologically relevant peptides.
Creighton
Christopher J
CJ
Johnson & Johnson Pharmaceutical Research and Development, Box 0776, Welsh and McKean Roads, Spring House, PA 19477-0776, USA. ccreight@prdus.jnj.com
Du
Yanming
Y
Santulli
Rosemary J
RJ
Tounge
Brett A
BA
Reitz
Allen B
AB
D008958:Models, Molecular; D018716:Molecular Mimicry; D009842:Oligopeptides / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology*
D009842:Oligopeptides; C047981:arginyl-glycyl-aspartic acid