Functional fibrils derived from the peptide TTR1-cycloRGDfK that target cell adhesion and spreading

Biomaterials

Volumn 32, Issue 26, 2011, Pages 6099-6110

  Bongiovanni, Marie N ^a,b   Scanlon, Denis B ^a   Gras, Sally L ^a,b  

^a UNIVERSITY OF MELBOURNE   (Australia)

^b UNIVERSITY OF MELBOURNE   (Australia)

Author keywords

Adhesion; Bioactivity; Cell spreading; Nanotopography; RGD peptide; Self assembly

Indexed keywords

AMYLOID-LIKE FIBRIL; BIOACTIVE PROPERTIES; CELL INTERACTION; CELL SPREADING; CORE STRUCTURE; FIBROUS NANOMATERIALS; INTEGRIN RECEPTORS; INTEGRINS; LOW LEVEL; MAMMALIAN CELLS; NANOTOPOGRAPHIES; NON-SPECIFIC INTERACTIONS; RGD PEPTIDE; SELF-ASSEMBLING; SPECIFIC INTERACTION;

ATOMIC FORCE MICROSCOPY; CELL ADHESION; CELL MEMBRANES; GLYCOPROTEINS; LIGANDS; MAMMALS; MATERIALS PROPERTIES; PEPTIDES; SCANNING ELECTRON MICROSCOPY; SELF ASSEMBLY; THIN FILMS;

ADHESION;

AMYLOID; ARGINYLGLYCYLASPARTIC ACID; ARGINYLGLYCYLASPARTYLPHENYLALANYLLYSINE; PENTAPEPTIDE; TTR1 CYCLORGDFK PEPTIDE; UNCLASSIFIED DRUG; VITRONECTIN RECEPTOR;

AMINO ACID SEQUENCE; ANIMAL CELL; ANIMAL TISSUE; ARTICLE; ATOMIC FORCE MICROSCOPY; CELL ADHESION; CELL INTERACTION; CELL SPREADING; CELL SURFACE; CONTROLLED STUDY; DEHYDRATION; FIBER; FILM; INFRARED RADIATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN INTERACTION; PROTEIN STRUCTURE; SCANNING ELECTRON MICROSCOPY; SYNCHROTRON; X RAY DIFFRACTION;

AMYLOID; ANIMALS; CELL ADHESION; CELL LINE; CELL MOVEMENT; HAPLORHINI; MICROSCOPY, ATOMIC FORCE; MICROSCOPY, ELECTRON, SCANNING; MICROSCOPY, ELECTRON, TRANSMISSION; MICROSCOPY, FLUORESCENCE; OLIGOPEPTIDES; SPECTROSCOPY, FOURIER TRANSFORM INFRARED;

MAMMALIA;

EID: 79959875103     PISSN: 01429612     EISSN: 18785905     Source Type: Journal    
DOI: 10.1016/j.biomaterials.2011.05.021     Document Type: Article

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