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Model peptides mimic the structure and function of the N‐terminus of the pore‐forming toxin sticholysin II by Fábio Casallanovo; Felipe J. F. de Oliveira; Fernando C. de Souza; Uris Ros; Yohanka Martínez; David Pentón; Mayra Tejuca; Diana Martínez; Fabiola Pazos; Thelma A. Pertinhez; Alberto Spisni; Eduardo M. Cilli; María E. Lanio; Carlos Alvarez; Shirley Schreier is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.
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## Abstract To investigate the role of the N‐terminal region in the lytic mechanism of the pore‐forming toxin sticholysin II (St II), we studied the conformational and functional properties of peptides encompassing the first 30 residues of the protein. Peptides containing residues 1–30 (P1–30) and 11–30 (P11–30) were synthesized and their conformational properties were examined in aqueous solution as a function of peptide concentration, pH, ionic strength, and addition of the secondary structure‐inducing solvent trifluoroethanol (TFE). CD spectra showed that increasing concentration, pH, and ionic strength led to aggregation of P1–30; as a consequence, the peptide acquired β‐sheet conformation. In contrast, P11–30 exhibited practically no conformational changes under the same conditions, remaining essentially structureless. Moreover, this peptide did not undergo aggregation. These differences clearly point to the modulating effect of the first 10 hydrophobic residues on the peptides aggregation and conformational properties. In TFE both the first ten hydrophobic peptides acquired α‐helical conformation, albeit to a different extent, P11–30 displayed lower α‐helical content. P1–30 p
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It is typically read by researchers, students, and practitioners in Biochemistry, Genetics and Molecular Biology.
- Author
- Fábio Casallanovo; Felipe J. F. de Oliveira; Fernando C. de Souza; Uris Ros; Yohanka Martínez; David Pentón; Mayra Tejuca; Diana Martínez; Fabiola Pazos; Thelma A. Pertinhez; Alberto Spisni; Eduardo M. Cilli; María E. Lanio; Carlos Alvarez; Shirley Schreier
- Publisher
- Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Wiley (ISSN 0006-3525)
- Published
- 2005
- Language
- EN
- Field
- Biochemistry, Genetics and Molecular Biology (Life Sciences)