Substrate-facilitated assembly of elastin-like peptides: studies by variable-temperature in situ atomic force microscopy.
Extended duration in situ variable-temperature atomic force microscopy performed on a series of coacervating hydrophobic peptides based on human elastin revealed a novel multistage surface assembly process. Formation of epitaxially arranged peptide rods was preceded by rapid expansion of a two-dimensional film on the nucleating substrate, a process facilitated by specific hydrophobic peptide-substrate and intrapeptide interactions.
Yang
Guocheng
G
Department of Chemical Engineering and Applied Chemistry, Institute of Biomaterials and Biomedical Engineering, 4 Taddle Creek Road, Toronto, Ontario, Canada M5S 3G9.
Woodhouse
Kimberly A
KA
Yip
Christopher M
CM
D001483:Base Sequence; D004549:Elastin / Q000096:biosynthesis / Q000138:chemical synthesis* / Q000737:chemistry / Q000235:genetics; D005091:Exons; D018625:Microscopy, Atomic Force; D010446:Peptide Fragments / Q000096:biosynthesis / Q000138:chemical synthesis* / Q000737:chemistry / Q000235:genetics; D017434:Protein Structure, Tertiary; D013499:Surface Properties; D013696:Temperature
D010446:Peptide Fragments; D004549:Elastin