title: Protein β-interfaces as a generic source of native peptide tectons.
abstract: Motifs of 7-8 amino acids were designed from the β-continuous interfaces of non-related homo-oligomeric proteins. These peptides intrinsically self-assembled into nanoarchitectures in water, while retaining some properties of their parent interfaces, especially reversibility of assembly. These results reveal a novel source of native peptide tectons.
authors: Biomolecular Interaction Centre, University of Canterbury, Private Bag 4800, Christchurch 8140, New Zealand. celine.valery@canterbury.ac.nz
authors: Céline
authors: C
authors: Valéry
authors: Rishi
authors: R
authors: Pandey
authors: Juliet A
authors: JA
authors: Gerrard
mesh_terms: D000818:Animals; D002262:Carboxy-Lyases / Q000737:chemistry* / Q000378:metabolism; D002417:Cattle; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism; D007782:Lactoglobulins / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D049329:Nanostructures / Q000737:chemistry*; D010446:Peptide Fragments / Q000737:chemistry*; D061105:Peroxiredoxin III / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D055503:Protein Multimerization; D014867:Water / Q000737:chemistry*
chemical_list: D029968:Escherichia coli Proteins; D007782:Lactoglobulins; D010446:Peptide Fragments; D014867:Water; D061105:Peroxiredoxin III; D002262:Carboxy-Lyases; C489812:LysA protein, E coli