title: Arbitrary self-assembly of peptide extracellular microscopic matrices.
abstract: Two faces for one matrix: A single bifaceted cyclopeptide block forms highly branched, porous, and intricate fibrillar networks, which span microscopic dimensions and mimic the extracellular matrix to support cell growth and proliferation. The peptide block has two domains connected with triglycine linkers (GGG); the domains consist of positively (blue) and negatively (red) charged heptads that provide interactions between different blocks.
authors: Department of Chemistry, University of Leicester, Leicester, LE1 7RH, UK.
authors: Angelo
authors: A
authors: Bella
authors: Santanu
authors: S
authors: Ray
authors: Michael
authors: M
authors: Shaw
authors: Maxim G
authors: MG
authors: Ryadnov
mesh_terms: D000595:Amino Acid Sequence; D002448:Cell Adhesion; D049109:Cell Proliferation; D005109:Extracellular Matrix / Q000737:chemistry*; D005347:Fibroblasts / Q000166:cytology; D006801:Humans; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry*; D010456:Peptides, Cyclic / Q000737:chemistry*; D016062:Porosity; D023822:Tissue Engineering; D054457:Tissue Scaffolds / Q000737:chemistry*
chemical_list: D009842:Oligopeptides; D010456:Peptides, Cyclic; C035647:glycyl-glycyl-glycine