Tuning β-sheet peptide self-assembly and hydrogelation behavior by modification of sequence hydrophobicity and aromaticity

Biomacromolecules

Volumn 12, Issue 7, 2011, Pages 2735-2745

  Bowerman, Charles J ^a   Liyanage, Wathsala ^a   Federation, Alexander J ^a   Nilsson, Bradley L ^a  

^a UNIVERSITY OF ROCHESTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID STRUCTURES; AROMATIC AMINO ACID; AROMATICITIES; CHARGE-CHARGE INTERACTIONS; DESIGN PRINCIPLES; ELECTROSTATIC COULOMBIC; FIBRIL FORMATION; FIBRILLAR HYDROGELS; HYDROGELATION; HYDROPHOBIC INTERACTIONS; NACL CONCENTRATION; NANORIBBONS; PROTONATED; RANDOM COIL; RELATIVE CONTRIBUTION; SECONDARY STRUCTURES; SELF ASSEMBLY PROCESS; SHEET FORMATION; WEAK GEL;

AMINO ACIDS; AROMATIC COMPOUNDS; AROMATIZATION; ASSEMBLY; BIOMATERIALS; GELS; GLYCOPROTEINS; HYDROGEN BONDS; HYDROPHOBICITY; IONIC STRENGTH; SELF ASSEMBLY; SODIUM CHLORIDE;

PEPTIDES;

AMYLOID; AROMATIC AMINO ACID; ISOLEUCINE; LEUCINE; LYSINE; PHENYLALANINE; SODIUM CHLORIDE; VALINE;

AMINO ACID SEQUENCE; ARTICLE; BETA SHEET; CHEMICAL INTERACTION; CHEMICAL MODIFICATION; CHEMICAL STRUCTURE; CIRCULAR DICHROISM; GELATION; HYDROGEN BOND; HYDROPHOBICITY; INFRARED SPECTROSCOPY; IONIC STRENGTH; PEPTIDE SYNTHESIS; PH MEASUREMENT; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTON NUCLEAR MAGNETIC RESONANCE; PROTON TRANSPORT; STATIC ELECTRICITY; TRANSMISSION ELECTRON MICROSCOPY;

AMINO ACIDS, AROMATIC; HYDROGELS; HYDROGEN-ION CONCENTRATION; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MOLECULAR STRUCTURE; OSMOLAR CONCENTRATION; PEPTIDES; PROTEIN STRUCTURE, SECONDARY; SODIUM CHLORIDE;

EID: 79960239994     PISSN: 15257797     EISSN: 15264602     Source Type: Journal    
DOI: 10.1021/bm200510k     Document Type: Article

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