期刊
PEPTIDES
卷 30, 期 5, 页码 866-872出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.peptides.2009.01.010
关键词
Conantokin peptides; Self-association; gamma-Carboxyglutamic acid; Dimerization; Strand alignment
资金
- China Natural Science Foundation [30672446, 90713028]
- High Technology Program of Oceans in China [2006AA09Z404]
- National Institutes of Health [HL019982]
We have previously found a new mode of metal ion-induced helix-helix assembly for the gamma-carboxyglutamate (Gla)-containing, neuroactive conantokin (con) peptides that is independent of the hydrophobic effect. In these unique metallo-zipper assemblies of con-G and con-T[K7 gamma], interhelical Ca(2+) coordination induces dimer formation with strictly antiparallel chain orientation in conantokin peptides in which Gla residues are positioned at i, i + 4, i + 7, i + 11 intervals. In order to probe the property of self-assembly in conantokin peptides with an extended Gla network, a con-T variant (con-T-tri) was synthesized that contains five Gla residues spaced at i, i + 4, i + 7, i + 11, i + 14 intervals. Sedimentation equilibrium analyses showed that Ca(2+), but not Mg(2+), was capable of promoting con-T-tri self-assembly. Oxidation and rearrangement assays with Cys-containing con-T-tri variants revealed that the peptide strands in the complex can orient in both parallel and antiparallel forms. Stable parallel and antiparallel dimeric forms of con-T-tri were modeled using disulfide-linked peptides and the biological viability of these species was confirmed by electrophysiology. These findings suggest that small changes within the helix-helix interface of the conantokins can be exploited to achieve desired modes of strand alignment. (C) 2009 Elsevier Inc. All rights reserved.
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