Binding mechanism of a de novo coiled coil complex elucidated from surface forces measurements.
J Colloid Interface Sci
; 581(Pt A): 218-225, 2021 Jan 01.
Article
en En
| 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.
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Colección:
01-internacional
Base de datos:
MEDLINE
Idioma:
En
Revista:
J Colloid Interface Sci
Año:
2021
Tipo del documento:
Article
País de afiliación:
Canadá