Vibrational (VCD) and electronic circular dichroism (ECD) spectroscopies were used to investigate non-covalent interactions between the cationic tripeptide L-lysyl-L-alanyl-L-alanine (KAA) and the anionic porphyrin meso-tetrakis(4-sulfonatophenyl)porphyrin (TPPS) in aqueous solution. Also studied were the interactions between KAA and the three metal derivatives of TPPS (copper(II), iron(III), and manganese(III)), each of which has a different number of axial ligands. VCD spectra in the amide I' ( C = O stretching vibration) region are extremely sensitive to peptide conformation, and, consequently, provide direct information about the conformational changes of host oligopeptide matrices caused by electrostatic interaction with guest porphyrin molecules. We found that pure KAA adopts a left-handed polyproline II (PPII) helical conformation when dissolved in aqueous solution at near-neutral pH values. When mixed with metal-free TPPS under the same conditions, VCD intensities were markedly reduced in the amide I' region and a new negative band was observed at 1634 cm−1; both findings indicating the transition of the PPII conformation into a less compact structure having similarities to β-sheet, herein termed a β-sheet-like conformation. In the case of the metal derivatives of TPPS studied, only variations in the VCD intensities in the amide I' region were observed. Compared to the results for pure KAA, the binding of Cu (II) TPPS , which has no axial ligand, resulted in the greatest decrease in amide I' VCD intensity. Nevertheless, the shape of a VCD spectrum characteristic for a PPII conformation was maintained, thereby indicating the presence of an “extended” PPII conformation in the Cu (II) TPPS -KAA complex. Conversely, Mn (III) TPPS , which has two axial ligands, did not significantly affect the PPII conformation of KAA in the Mn (III) TPPS -KAA complex. The effects of the metalation and axial ligation of TPPS on the conformation of KAA in peptide-porphyrin complexes are discussed, together with the results of our ECD study.
Subunit association and structural analysis of platelet basic protein and related proteins investigated by 1H NMR spectroscopy and circular dichroism.
