title: Exploitable length correlations in peptide nanofibres.
abstract: Sequence-prescribed biomolecular assemblies find increasing use in the development of novel nanostructured materials. Critical requirements for emerging designs remain in matching form with function. Peptide assembly diversifies form and supports function, but lacks control over both. Herein we exploit length correlations in peptide nanoscale fibres (form) using a model helical template. We establish that different assembly patterns result from a synergistic interplay between peptide length, net charge and folding and supra-molecular cooperativity, while correlating with increases in cell proliferation (function) as a function of peptide length. The revealed correlations offer an efficient rationale for the programming of longitudinally finite and biologically active nanoscale fibres.
authors.affiliation: National Physical Laboratory, Hampton Road, Teddington, Middlesex TW11 0LW, UK. max.ryadnov@npl.co.uk.
authors.forename: Emiliana
authors.initials: E
authors.lastname: De Santis
authors.forename: Nilofar
authors.initials: N
authors.lastname: Faruqui
authors.forename: James E
authors.initials: JE
authors.lastname: Noble
authors.forename: Maxim G
authors.initials: MG
authors.lastname: Ryadnov
mesh_terms: D000595:Amino Acid Sequence; D002448:Cell Adhesion / Q000502:physiology*; D016764:Cell Polarity / Q000502:physiology; D049109:Cell Proliferation / Q000502:physiology*; D002478:Cells, Cultured; D005347:Fibroblasts / Q000166:cytology / Q000502:physiology*; D006801:Humans; D008969:Molecular Sequence Data; D057139:Nanofibers / Q000737:chemistry* / Q000648:ultrastructure*; D010316:Particle Size; D010455:Peptides / Q000737:chemistry*
chemical_list: D010455:Peptides