In this work we examine the binding and folding of the membrane-active peptide, melittin in the presence of ganglioside GM1 micelle. The membrane bilayer is capable of inducing folding to small proteins and peptides upon binding. Using two-dimensional NMR techniques we have shown that at low concentration, GM1 micelle is able to induce an extended helical conformation to MLT. The pulsed-field gradient diffusion NMR study indicates that the peptide partition into GM1 micelle along with about 32% binding. While looking for the binding between MLT and GM1 using saturation transfer difference NMR spectroscopy, Val⁵, Leu⁹, Thr¹¹, Ile¹⁷, Ser¹⁸, and Trp¹⁹ have been identified as the residues that are in close proximity to GM1 micelles.

Key words: Melittin; GM1; Micelle; PFG-SE; STD-NMR; NOESY; and Restrained molecular dynamics.