title: Molecular modeling of hair keratin/peptide complex: Using MM-PBSA calculations to describe experimental binding results.
abstract: Molecular dynamics simulations of a keratin/peptide complex have been conducted to predict the binding affinity of four different peptides toward human hair. Free energy calculations on the peptides' interaction with the keratin model demonstrated that electrostatic interactions are believed to be the main driving force stabilizing the complex. The molecular mechanics-Poisson-Boltzmann surface area methodology used for the free energy calculations demonstrated that the dielectric constant in the protein's interior plays a major role in the free energy calculations, and the only way to obtain accordance between the free energy calculations and the experimental binding results was to use the average dielectric constant.
authors.affiliation: Departamento de Engenharia Têxtil, Universidade do Minho, Campus de Azurém, 4800-058 Guimarães, Portugal.
authors.forename: Nuno G
authors.initials: NG
authors.lastname: Azoia
authors.forename: Margarida M
authors.initials: MM
authors.lastname: Fernandes
authors.forename: Nuno M
authors.initials: NM
authors.lastname: Micaêlo
authors.forename: Cláudio M
authors.initials: CM
authors.lastname: Soares
authors.forename: Artur
authors.initials: A
authors.lastname: Cavaco-Paulo
mesh_terms: D000595:Amino Acid Sequence; D006801:Humans; D053564:Keratins, Hair-Specific / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D056004:Molecular Dynamics Simulation; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry* / Q000378:metabolism; D037663:Pulmonary Surfactant-Associated Protein D / Q000737:chemistry / Q000378:metabolism; D055672:Static Electricity; D013816:Thermodynamics
chemical_list: D053564:Keratins, Hair-Specific; D010446:Peptide Fragments; D037663:Pulmonary Surfactant-Associated Protein D