[Conformational aspects of the molecular mechanism of action of bradykinin. II. Conformation and selectivity of action of bradykinin cycloanalogs].

Conformation energy calculations performed for cyclo[(epsilon-lysine1, glycine6)]bradykinin and cyclo-epsilon-kallidin indicate the absence of spatially equivalent low-energy structures for bradykinin and cyclobradykinin molecules, whereas cyclokallidin has conformations similar to the "biologically active" ones for bradykinin that are implicated in binding to both B1 and B2 type receptors.