It is known that, while melittin at micromolar concentrations is unfolded under conditions of low ionic strength at neutral pH, it adopts a tetrameric alpha-helical structure under conditions of high ionic strength, at alkaline pH, or at high peptide concentrations. To understand the mechanism of the conformational transition of melittin, we examined in detail the conformation of melittin under various conditions by far-UV circular dichroism at 20 degrees C. We found that the helical conformation is also stabilized by strong acids such as perchloric acid. The effects of various acids varied largely and were similar to those of the corresponding salts, indicating that the anions are responsible for the salt- or acid-induced transitions. The order of effectiveness of various monovalent anions was consistent with the electroselectivity series of anions toward anion-exchange resins, indicating that the anion binding is responsible for the salt- or acid-induced transitions. From the NaCl-, HCl-, and alkaline pH-induced conformational transitions, we constructed a phase diagram of the anion- and pH-dependent conformational transition. The phase diagram was similar in shape to that of acid-denatured apomyoglobin [Goto, Y., & Fink, A.L. (1990) J. Mol. Biol. 214, 803-805] or that of the amphiphilic Lys, Leu model polypeptide [Goto, Y., & Aimoto, S. (1991) J. Mol. Biol. 218, 387-396], suggesting a common mechanism of the conformational transition. The anion-, pH-, and peptide concentration-dependent conformational transition of melittin was explained on the basis of an equation in which the conformational transition is linked to proton and anion binding to the titratable groups. Study holds ProTherm entries: 3971 Extra Details: alpha-helical structure; conformational transition ;,electroselectivity; phase diagram; anion binding
Submitter: Connie Wang
Submission Date: April 24, 2018, 8:23 p.m.
|Structure ID||Release Date||Resolution||Structure Title|
|2MW6||2015-07-01||Structure of the bee venom toxin melittin with [(C5H5)Ru]+ fragment attached to the tryptophan residue|
|1BH1||1999-01-06||STRUCTURAL STUDIES OF D-PRO MELITTIN, NMR, 20 STRUCTURES|
|3QRX||2011-10-26||2.2||Chlamydomonas reinhardtii centrin bound to melittin|
|Percent Identity||Matching Chains||Protein||Accession||Entry Name|