Interpretation of the dissolution of insoluble peptide sequences based on the acid-base properties of the solvent

Interpretation of the dissolution of insoluble peptide sequences based on the acid-base properties of the solvent

Autor Malavolta, Luciana Autor UNIFESP Google Scholar
Pinto, Marcelo RS Google Scholar
Cuvero, Jamile H. Google Scholar
Nakaie, Clovis Ryuichi Autor UNIFESP Google Scholar
Instituição Universidade Federal de São Paulo (UNIFESP)
Resumo The dissolution process of model insoluble peptide sequences was investigated in view of the electron acceptor ( AN) and electron donor (DN) solvent properties. the Alzheimer's disease-inducing (1-42) A beta-amyloid peptide and its (1-21) fragment, the (66-97) transmembrane bradykinin B2 receptor sequence, and the strongly aggregated VVLGAAIV were selected as models of insoluble peptides. Solvents presenting similar AN and DN values failed, despite their polarities, to dissociate peptide chains ( free in solution or bound to a polymer). the maximum solubility of these aggregated sequences was attained in solvents presenting the highest possible (AN-DN) values ( in positive or negative mode). the AN-DN values ranged from approximately -20 to +80 and, notably, the lowest dissociation power was ascribed to solvents presenting values of approximately +40. the strong hydrogen bond donor water is located in this region, indicating that, for dissociation of specific insoluble segments, the solvent should appropriately combine its acid/base strength with the potential for van der Waals interactions. We also observed a sequence-dependent pH effect on peptide solubility confirmed through circular dichroism spectroscopy. This approach also revealed a complex but, in many cases, consistent influence of peptide conformation on its solubility degree, even when structure-inducing solvents were added. in conclusion, the random method of selecting solvents to dissolve insoluble and intractable peptide sequences, still in use by some, could be partially supplanted by the strategy described herein, which may be also applicable to other solute dissociation processes.
Assunto peptide
solvent property
Alzheimer's disease
Idioma Inglês
Data 2006-06-01
Publicado em Protein Science. Woodbury: Cold Spring Harbor Lab Press, Publications Dept, v. 15, n. 6, p. 1476-1488, 2006.
ISSN 0961-8368 (Sherpa/Romeo, fator de impacto)
Editor Cold Spring Harbor Lab Press, Publications Dept
Extensão 1476-1488
Direito de acesso Acesso aberto Open Access
Tipo Artigo
Web of Science WOS:000237927900023

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