Self-complementary synthetic peptides, composed by 8 and 16 residues, were analyzed by CD, NMR and small angle neutron scattering (SANS) techniques in order to investigate the relevance of charge and hydrophobic interactions in determining their self-assembling properties. All the sequences are potentially able to form fibrils and membranes as they share, with the prototype EAK16, a strictly alternating arrangement of polar and nonpolar residues. We find that 16-mer peptides show higher self-assembling propensities than the 8-mer analogs and that the aggregation processes are favored by salts and neutral pH. Peptide hydrophobic character appears as the most relevant factor in determining self-assembling. Solution conformational analysis, diffusion and SANS measurements all together show that the sequences with a higher self-assemble propensity are distributed, in mild conditions, between light and heavy forms. For some of the systems, the light form is mostly constituted by monomers in a random conformation, while the heavy one is constituted by β-aggregates. In our study we also verified that sequences designed to adopt extended conformation, when dissolved in alcohol-water mixtures, can easily fold in helix structures. In that media, the prototype of the series appears distributed between helical monomers and β-aggregates. It is worth noticing that the structural conversion from helical monomer to β-aggregates, mimics β-amyloid peptide aggregation mechanisms. Copyright_c 2008 European Peptide Society and JohnWiley & Sons, Ltd.
Self-assembling of ionic-complementary peptides / D'Auria, Gabriella; Vacatello, M. a.; Falcigno, Lucia; Paduano, Luigi; G., Mangiapia; L., Calvanese; R., Gambaretto; M., Dettin; L., Paolillo. - In: JOURNAL OF PEPTIDE SCIENCE. - ISSN 1075-2617. - ELETTRONICO. - 15:(2009), pp. 210-219. [10.1002/psc.1083]
Self-assembling of ionic-complementary peptides
D'AURIA, GABRIELLA;FALCIGNO, LUCIA;PADUANO, LUIGI;
2009
Abstract
Self-complementary synthetic peptides, composed by 8 and 16 residues, were analyzed by CD, NMR and small angle neutron scattering (SANS) techniques in order to investigate the relevance of charge and hydrophobic interactions in determining their self-assembling properties. All the sequences are potentially able to form fibrils and membranes as they share, with the prototype EAK16, a strictly alternating arrangement of polar and nonpolar residues. We find that 16-mer peptides show higher self-assembling propensities than the 8-mer analogs and that the aggregation processes are favored by salts and neutral pH. Peptide hydrophobic character appears as the most relevant factor in determining self-assembling. Solution conformational analysis, diffusion and SANS measurements all together show that the sequences with a higher self-assemble propensity are distributed, in mild conditions, between light and heavy forms. For some of the systems, the light form is mostly constituted by monomers in a random conformation, while the heavy one is constituted by β-aggregates. In our study we also verified that sequences designed to adopt extended conformation, when dissolved in alcohol-water mixtures, can easily fold in helix structures. In that media, the prototype of the series appears distributed between helical monomers and β-aggregates. It is worth noticing that the structural conversion from helical monomer to β-aggregates, mimics β-amyloid peptide aggregation mechanisms. Copyright_c 2008 European Peptide Society and JohnWiley & Sons, Ltd.File | Dimensione | Formato | |
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