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.
Chatterjee
Chiradip
C
Department of Chemistry, University of Calcutta 92, A.P.C. Road, Kolkata 700 009, India.
Mukhopadhyay
Chaitali
C
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