title: Ionic peptide aggregation: exploration of conformational dynamics in aqueous solution by computational techniques.
abstract: The effects of end groups on KEK peptide conformational characteristics and self-assembling properties in water solution are investigated by using long lasting all-atom molecular dynamics simulations. The analysis of the structural macroscopic and microscopic properties and the examination of intra- and intermolecular interactions suggest, in agreement with experimental observations, the role played by side chains and terminal regions in determining the characteristic features of the assemblages. Competition between intra- and interchain interactions greatly affects the diffusivity of peptide molecules and the conformational space that they can sample, ultimately controlling the shape, size, and distribution of the aggregate configurations. Different peptide end groups influence peptide flexibility and seem to play a crucial role in determining the aggregates' supramolecular architectures.
authors.affiliation: Dipartimento di Chimica e Chimica Industriale, Universita degli Studi di Pisa, Via Risorgimento 35, I-56126 Pisa, Italy.
authors.forename: Celia
authors.initials: C
authors.lastname: Duce
authors.forename: Susanna
authors.initials: S
authors.lastname: Monti
authors.forename: Roberto
authors.initials: R
authors.lastname: Solaro
authors.forename: Maria Rosaria
authors.initials: MR
authors.lastname: Tiné
mesh_terms: D003198:Computer Simulation; D006860:Hydrogen Bonding; D007477:Ions / Q000737:chemistry; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D012680:Sensitivity and Specificity; D012996:Solutions / Q000737:chemistry; D013997:Time Factors; D014867:Water / Q000737:chemistry
chemical_list: D007477:Ions; D010455:Peptides; D012996:Solutions; D014867:Water