Interaction and structural study of kinin peptide bradykinin and ganglioside monosialylated 1 micelle.
Partitioning of small proteins and peptides from the aqueous to membrane phase is often coupled with folding. In this work we examine the binding and folding of the kinin peptide, bradykinin (BK), in the presence of the ganglioside monosialylated 1 (GM1) micelle. Using two-dimensional NMR techniques, we have shown that at low concentration, GM1 micelle is able to induce a turn conformation to BK. A pulsed-field gradient diffusion NMR study indicated that the peptide partitions into the GM1 micelle with a DeltaG(part) of -3.14 +/- 0.03 kcal/mol. A saturation transfer difference (STD) NMR study indicated that the binding is mostly through hydrophobic residues.
Chatterjee
Chiradip
C
Department of Chemistry, University of Calcutta, 92, A. P. C. Road, Kolkata-700 009, India.
Mukhopadhyay
Chaitali
C
D000595:Amino Acid Sequence; D001920:Bradykinin / Q000737:chemistry* / Q000378:metabolism*; D004058:Diffusion; D018604:Epitope Mapping; D005677:G(M1) Ganglioside / Q000737:chemistry* / Q000378:metabolism*; D057927:Hydrophobic and Hydrophilic Interactions; D008823:Micelles; D008958:Models, Molecular; D008968:Molecular Conformation; D019906:Nuclear Magnetic Resonance, Biomolecular; D011485:Protein Binding; D011487:Protein Conformation; D017510:Protein Folding; D011522:Protons; D014867:Water / Q000737:chemistry
D008823:Micelles; D011522:Protons; D014867:Water; D005677:G(M1) Ganglioside; D001920:Bradykinin