Self-association of disulfide-dimerized melittin analogues

Biochemistry
J TakeiC E Dempsey

Abstract

Two cysteine substitutions of bee venom melittin have been synthesized to investigate the effects of disulfide cross-linking on the self-association properties of the peptide in solution. K23C melittin (mltK23C) was designed to link nonpolar surfaces of the amphipathic melittin helix on the basis of the close juxtaposition of pairs of K23 side chains in the crystal of the native melittin tetramer. K23Q/Q25C melittin (mltQ25C) was designed to link the polar surfaces of the peptide such that self-association in membrane bound states might be stabilized. The mltK23C disulfide dimer, (mltK23C)2, is highly structured at low pH under conditions where native melittin, and the mltK23C monomer, are unstructured. High-resolution NMR, circular dichroism, and fluorescence spectroscopy established that (mltK23C)2 is a helical monomer (pseudodimer) with stable helical segments between residues 2-13 and 15-25. Although the symmetrical nature of the pseudodimer prevented high-resolution structure determination, analysis of calculated hydrogen bond lengths, chemical shifts, near-UV circular dichroism, and urea denaturation demonstrated similarities with alpha-helical coiled coils and with the structure of native melittin in methanol. Stopped fl...Continue Reading

References

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May 7, 1990·Biochimica Et Biophysica Acta·C E Dempsey
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Mar 1, 1994·Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire·J D Baleja, B D Sykes
Aug 1, 1985·Biophysical Journal·D SchubertK Boss

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Citations

Jul 20, 2006·Bioconjugate Chemistry·Chang-Po ChenKevin G Rice
Jun 27, 2012·Journal of the American Chemical Society·Aram J KrausonWilliam C Wimley
Sep 10, 2014·Amino Acids·Elaheh JamasbiMohammed Akhter Hossain
Mar 27, 2007·Journal of Colloid and Interface Science·Adam A StrömstedtMartin Malmsten
Mar 30, 2001·The Journal of Biological Chemistry·J OrivelJ Rossier

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