Post-assembly functionalization of supramolecular nanostructures with bioactive peptides and fluorescent proteins by native chemical ligation

Bioconjugate Chemistry

Volumn 25, Issue 4, 2014, Pages 707-717

  Khan, Saahir ^a,b,c   Sur, Shantanu ^a   Dankers, Patricia Y W ^a,d   Da Silva, Ricardo M P ^a,d   Boekhoven, Job ^a   Poor, Taylor A ^a,c   Stupp, Samuel I ^a,b,c  

^a NORTHWESTERN UNIVERSITY   (United States)

^b Northwestern University   (United States)

^c NORTHWESTERN UNIVERSITY   (United States)

^d EINDHOVEN UNIVERSITY OF TECHNOLOGY   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

CELL CULTURE; ELECTROPHORETIC MOBILITY; ENERGY TRANSFER; FLUORESCENCE; GOLD NANOPARTICLES; MOLECULES; NANOFIBERS; PEPTIDES; POLYSTYRENES; SELF ASSEMBLY; SUPRAMOLECULAR CHEMISTRY;

AMPHIPHILE MOLECULES; BIOACTIVE PEPTIDES; FUNCTIONALIZATIONS; LIGATION REACTIONS; NATIVE CHEMICAL LIGATION; PEPTIDE AMPHIPHILES; PEPTIDE PROTEINS; RGDS PEPTIDES; SELF-ASSEMBLED PEPTIDES; SUPRA-MOLECULAR NANO STRUCTURES;

BIOACTIVITY;

AMPHOPHILE; ARGINYLGLYCYLASPARTYLSERINE; CYAN FLUORESCENT PROTEIN; GOLD NANOPARTICLE; NANOFIBER; NANOMATERIAL; PEPTIDE AMPHIPHILE; STREPTAVIDIN; UNCLASSIFIED DRUG; YELLOW FLUORESCENT PROTEIN; MACROMOLECULE; PEPTIDE; PHOTOPROTEIN;

ANISOTROPY; ARTICLE; BIOLOGICAL ACTIVITY; CELL STRUCTURE; CHEMICAL REACTION; CONJUGATION; COVALENT BOND; ELECTROPHORETIC MOBILITY; ENERGY TRANSFER; FIBROBLAST; FORSTER RESONANCE ENERGY TRANSFER; IMMOBILIZATION; NATIVE CHEMICAL LIGATION; OBSERVATION; PROTEIN IMMOBILIZATION; PROTEIN STRUCTURE; 3T3 CELL LINE; ANIMAL; CELL CULTURE; CELL SURVIVAL; CHEMICAL STRUCTURE; CHEMISTRY; CYTOLOGY; MACROMOLECULE; METABOLISM; MOUSE; PARTICLE SIZE; SURFACE PROPERTY; SYNTHESIS;

ANIMALS; CELL SURVIVAL; CELLS, CULTURED; FIBROBLASTS; LUMINESCENT PROTEINS; MACROMOLECULAR SUBSTANCES; MICE; MODELS, MOLECULAR; MOLECULAR STRUCTURE; NANOSTRUCTURES; NIH 3T3 CELLS; PARTICLE SIZE; PEPTIDES; SURFACE PROPERTIES;

EID: 84898946447     PISSN: 10431802     EISSN: 15204812     Source Type: Journal    
DOI: 10.1021/bc400507v     Document Type: Article

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