Melittin-GM1 interaction: a model for a side-by-side complex

Biochemical and Biophysical Research Communications
Chiradip Chatterjee, Chaitali Mukhopadhyay

Abstract

We report here the interaction of melittin with ganglioside GM1 by steady-state fluorescence, one-dimensional (1)H NMR spectroscopy and molecular modeling. In the presence of GM1 the emission maximum of melittin is blue shifted and fluorescence quenching efficiencies of iodide and acrylamide are substantially reduced, indicating a shielding of tryptophan of melittin from aqueous environment. Significant line broadening of NMR resonances of melittin, suggestive of motional restriction, is observed. Molecular modeling indicates a melittin-GM1 complex with N-terminal hydrophobic stretch of melittin associating with the ceramide tail and C-terminal hydrophilic end of melittin having favorable electrostatic interaction with the carbohydrate head group of GM1.

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Citations

Jun 27, 2012·Journal of the American Chemical Society·Aram J KrausonWilliam C Wimley
Dec 4, 2003·Biopolymers·Chiradip Chatterjee, Chaitali Mukhopadhyay
Aug 3, 2005·Journal of Biomolecular Structure & Dynamics·Chiradip Chatterjee, Chaitali Mukhopadhyay
Nov 26, 2019·Protein Science : a Publication of the Protein Society·Lisa M RamirezJayanti Pande
Nov 16, 2019·The Journal of Membrane Biology·Zarrin Shahzadi, Chaitali Mukhopadhyay
Sep 17, 2009·Langmuir : the ACS Journal of Surfaces and Colloids·Moutusi Manna, Chaitali Mukhopadhyay
Feb 27, 2004·Biochemical and Biophysical Research Communications·Chiradip Chatterjee, Chaitali Mukhopadhyay
Sep 4, 2018·Langmuir : the ACS Journal of Surfaces and Colloids·Zarrin ShahzadiChaitali Mukhopadhyay
Jan 10, 2019·Chemical Reviews·Shantanu GuhaWilliam C Wimley
Oct 13, 2010·Biochimica Et Biophysica Acta·Anindita GayenChaitali Mukhopadhyay

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