Pm. Doyle et al., SOLUTION STRUCTURE OF A BIOLOGICALLY-ACTIVE CYCLIC LDV PEPTIDE ANALOGCONTAINING A TYPE II' BETA-TURN MIMETIC, International journal of peptide & protein research, 47(6), 1996, pp. 427-436
The solution structure of cyclo-[Gly-Leu-Asp-Val-BTD] (BTD = p-turn di
peptide) has been determined by two-dimensional H-1-NMR (nuclear magne
tic resonance) spectroscopy and systematic conformational searching co
mbined with molecular dynamics studies. The structure contains two hyd
rogen bonds between the Gly and Val residues, and a type I beta-turn w
ith Leu and Asp at the (i+1) and (i+2) positions of the turn, The cycl
ic compound shows activity in a scintillation proximity assay (SPA) fo
r the inhibition of the interaction between the integrin alpha(4) beta
(1) and vascular cell adhesion molecule-1 (VCAM-1), The structure-acti
vity relationship of the LDV sequence is discussed. (C) Munksgaard 199
6.