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Towards an experimental classification system for membrane active peptides.
Brand, G D; Ramada, M H S; Genaro-Mattos, T C; Bloch, C.
Affiliation
  • Brand GD; Laboratório de Espectrometria de Massa, Embrapa Recursos Genéticos e Biotecnologia, Brasília, DF, Brazil.
  • Ramada MHS; Laboratório de Síntese e Análise de Biomoléculas, Instituto de Química, Universidade de Brasília, Brasília, DF, Brazil.
  • Genaro-Mattos TC; Laboratório de Espectrometria de Massa, Embrapa Recursos Genéticos e Biotecnologia, Brasília, DF, Brazil.
  • Bloch C; Departamento de Biologia Celular, Instituto de Ciências Biológicas, Universidade de Brasília, Brasília, DF, Brazil.
Sci Rep ; 8(1): 1194, 2018 01 19.
Article in En | MEDLINE | ID: mdl-29352252
Mature proteins can act as potential sources of encrypted bioactive peptides that, once released from their parent proteins, might interact with diverse biomolecular targets. In recent work we introduced a systematic methodology to uncover encrypted intragenic antimicrobial peptides (IAPs) within large protein sequence libraries. Given that such peptides may interact with membranes in different ways, resulting in distinct observable outcomes, it is desirable to develop a predictive methodology to categorize membrane active peptides and establish a link to their physicochemical properties. Building upon previous work, we explored the interaction of a range of IAPs with model membranes probed by differential scanning calorimetry (DSC) and circular dichroism (CD) techniques. The biophysical data were submitted to multivariate statistical methods and resulting peptide clusters were correlated to peptide structure and to their antimicrobial activity. A re-evaluation of the physicochemical properties of the peptides was conducted based on peptide cluster memberships. Our data indicate that membranolytic peptides produce characteristic thermal transition (DSC) profiles in model vesicles and that this can be used to categorize novel molecules with unknown biological activity. Incremental expansion of the model presented here might result in a unified experimental framework for the prediction of novel classes of membrane active peptides.
Subject(s)

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Cell Membrane / Antimicrobial Cationic Peptides Type of study: Prognostic_studies Limits: Humans Language: En Journal: Sci Rep Year: 2018 Document type: Article Affiliation country: Brasil Country of publication: Reino Unido

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Cell Membrane / Antimicrobial Cationic Peptides Type of study: Prognostic_studies Limits: Humans Language: En Journal: Sci Rep Year: 2018 Document type: Article Affiliation country: Brasil Country of publication: Reino Unido