PMID: 7538789May 4, 1995Paper

Conformation, pore-forming activity, and antigenicity of synthetic peptide analogues of a spiralin putative amphipathic alpha helix

Biochimica Et Biophysica Acta
C BrennerH Wróblewski

Abstract

Current models depict spiralin as a bitopic transmembrane protein with the transbilayer domain being an amphipathic alpha helix. However, though secondary structure prediction methods suggest a helical conformation for the hypothetical transmembrane segment of spiralin, no potential transmembrane helices could be detected in this protein using the method of Von Heijne (Von Heijne, G. (1992) J. Mol. Biol. 225, 487-494). Therefore, we have reconsidered the spiralin topological model by investigating the properties of the chemically synthesized peptides SM-BC3 (LNAVNTYATLAKAVLDAIQN-NH2) and SC-R8A2 (LNAVNTYATLASAVLEAIKN-NH2), corresponding to the hypothetical transmembrane segments of spiralins of two distinct spiroplasma species. The hydrophobic moment plot method suggests that these spiralin amino acid stretches are class G amphipathic alpha helices (i.e., helices localized on the surface of a globular protein domain). Circular dichroism spectra showed that both peptides have little ordered structure in aqueous solutions but adopt a mainly helical conformation in the presence of 25% trifluoroethanol or in detergent micelles (up to 74% alpha helix). Both peptides formed concentration- and voltage-dependent pores in planar lipid b...Continue Reading

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Citations

Sep 20, 2006·Journal of Molecular Microbiology and Biotechnology·Shlomo Trachtenberg
Apr 2, 2002·Protein Expression and Purification·Michel Le HénaffCatherine Fontenelle
Mar 2, 1999·Journal of Structural Biology·S Trachtenberg
Dec 5, 1998·Microbiology and Molecular Biology Reviews : MMBR·S RazinY Naot

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