Conformational alteration of bradykinin in presence of GM1 micelle.
We report here the interaction of bradykinin with ganglioside GM1 by circular dichroism, steady-state fluorescence, and one-dimensional 1H NMR spectroscopy. Circular dichroism spectroscopy is indicative of a turn formation of bradykinin backbone in the presence of GM1 micelle. The fluorescence quenching efficiencies of iodide and acrylamide are substantially reduced, indicating a shielding of phenylalanine residue of bradykinin from aqueous environment. Significant line broadening of NMR resonances of bradykinin, suggestive of motional restriction, is observed.
Department of Chemistry, University of Calcutta 92, A.P.C. Road, Kolkata 700 009, India.
Chiradip
C
Chatterjee
Chaitali
C
Mukhopadhyay
D000818:Animals; D001920:Bradykinin / Q000737:chemistry*; D002942:Circular Dichroism; D005677:G(M1) Ganglioside / Q000737:chemistry* / Q000494:pharmacology; D006041:Goats; D008823:Micelles; D019906:Nuclear Magnetic Resonance, Biomolecular; D010649:Phenylalanine / Q000737:chemistry; D011487:Protein Conformation; D013050:Spectrometry, Fluorescence; D017186:Titrimetry
D008823:Micelles; D005677:G(M1) Ganglioside; D010649:Phenylalanine; D001920:Bradykinin