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Default Solution NMR Structure and Backbone Dynamics of Recombinant Bee Venom Melittin.

Solution NMR Structure and Backbone Dynamics of Recombinant Bee Venom Melittin.

Related Articles Solution NMR Structure and Backbone Dynamics of Recombinant Bee Venom Melittin.

Biochemistry. 2018 Apr 18;:

Authors: Ramirez L, Shekhtman A, Pande J

Abstract
In recent years there has been a resurgence of interest in melittin and its variants as their therapeutic potential has become increasingly evident. Melittin is a 26-residue peptide and a toxic component of honey bee venom. The versatility of melittin in interacting with various biological substrates, such as membranes, glycosaminoglycans and a variety of proteins has inspired a slew of studies to understand the structural basis of such interactions. However, these studies have largely focused on melittin solutions at high concentrations (> 1mM), even though melittin is generally effective at lower, (micromolar) concentrations. Here we present high-resolution NMR studies in the lower concentration regime using a novel method to produce isotope labeled (15N, 13C) recombinant melittin. We provide residue-specific structural characterization of melittin in dilute aqueous solution and in TFE-water mixtures, which mimic melittin structure-function and interactions in aqueous, and membrane-like environments respectively. We find that the cis-trans isomerization of Pro14 is key to changes in the secondary structure of melittin. Thus, this study provides residue-specific structural information on melittin in the free-state and in a model of the substrate-bound state. These results, taken together with published work from other labs, reveal the peptide's structural versatility which resembles that of intrinsically disordered proteins and peptides.


PMID: 29668274 [PubMed - as supplied by publisher]



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