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Binding mechanism of a de novo coiled coil complex elucidated from surface forces measurements.
Shrestha, Buddha R; Liberelle, Benoit; Murschel, Frederic; Purisima, Enrico O; Sulea, Traian; De Crescenzo, Gregory; Banquy, Xavier.
Afiliação
  • Shrestha BR; Canada Research Chair in Bio-Inspired Materials and Interfaces, Faculty of Pharmacy, Université de Montréal, Montréal, Québec, Canada.
  • Liberelle B; Department of Chemical Engineering, Groupe de Recherche en Sciences et Technologie Biomédicales (GRSTB), Bio-P2 Research Unit, École Polytechnique de Montréal, Montréal, Québec H3C 3A7, Canada.
  • Murschel F; Department of Chemical Engineering, Groupe de Recherche en Sciences et Technologie Biomédicales (GRSTB), Bio-P2 Research Unit, École Polytechnique de Montréal, Montréal, Québec H3C 3A7, Canada.
  • Purisima EO; Human Health Therapeutics Research Centre, National Research Council Canada, Montréal, Québec, Canada.
  • Sulea T; Human Health Therapeutics Research Centre, National Research Council Canada, Montréal, Québec, Canada.
  • De Crescenzo G; Department of Chemical Engineering, Groupe de Recherche en Sciences et Technologie Biomédicales (GRSTB), Bio-P2 Research Unit, École Polytechnique de Montréal, Montréal, Québec H3C 3A7, Canada. Electronic address: gregory.decrescenzo@polymtl.ca.
  • Banquy X; Canada Research Chair in Bio-Inspired Materials and Interfaces, Faculty of Pharmacy, Université de Montréal, Montréal, Québec, Canada. Electronic address: xavier.banquy@umontreal.ca.
J Colloid Interface Sci ; 581(Pt A): 218-225, 2021 Jan 01.
Artigo em Inglês | MEDLINE | ID: mdl-32771733
ABSTRACT
We used the Surface Forces Apparatus to elucidate the interaction mechanism between grafted 5 heptad-long peptides engineered to spontaneously form a heterodimeric coiled-coil complex. The results demonstrated that when intimate contact between peptides is reached, binding occurs first via weakly interacting but more mobile distal heptads, suggesting an induced-fit association process. Precise control of the distance between peptide-coated surfaces allowed to quantitatively monitor the evolution of their biding energy. The binding energy of the coiled-coil complex increased in a stepwise fashion rather than monotonically with the overlapping distance, each step corresponding to the interaction between a quantized number of heptads. Surface forces data were corroborated to surface plasmon resonance measurements and molecular dynamics simulations and allowed the calculation of the energetic contribution of each heptad within the coiled-coil complex.
Texto completo: Disponível Coleções: Bases de dados internacionais Base de dados: MEDLINE Idioma: Inglês Revista: J Colloid Interface Sci Ano de publicação: 2021 Tipo de documento: Artigo País de afiliação: Canadá

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Texto completo: Disponível Coleções: Bases de dados internacionais Base de dados: MEDLINE Idioma: Inglês Revista: J Colloid Interface Sci Ano de publicação: 2021 Tipo de documento: Artigo País de afiliação: Canadá