Conformational Features of Bradykinin

Abstract
The circular dichroism (CD) of the peptide hormone bradykinin and its analogs, [Phe(H4)5]bradykinin, [Phe(H4)8]bradykinin, [Phe(H4)5,8]bradykinin, [TyrOMe5]bradykinin, [TyrOMe8]bradykinin, and [TyrOMe5,8]bradykinin, is described. The comparison of the CD spectra of these analogs with each other, recorded under a variety of conditions (pH, solvent, temperature), allows the monitoring of the behavior of the aromatic side-chains (phenylalanine, tyrosine) and an estimation of their respective spectral contributions in both spectral regions (320-250 nm, 250-190 nm) with good precision. Conformational non-equivalence of the residues Phe-5 and Phe-8 together with some overall conformational features of bradykinin are established.