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Site‐Specific Protein and Peptide Immobilization on a Biosensor Surface by Pulsed Native Chemical Ligation
Author(s) -
Helms Brett,
van Baal Ingrid,
Merkx Maarten,
Meijer E. W.
Publication year - 2007
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200700355
Subject(s) - biomolecule , chemoselectivity , native chemical ligation , peptide , biosensor , chemistry , cysteine , combinatorial chemistry , homogeneous , analyte , click chemistry , microfluidics , ligand (biochemistry) , nanotechnology , materials science , biochemistry , chromatography , enzyme , physics , receptor , thermodynamics , catalysis
Microfluidic biosensor chips that are functionalized with cysteine derivatives are readily modified with peptides and proteins by pulsed native chemical ligation. The chemoselectivity ensures a homogeneous presentation of the biomolecule at the surface, and the ligand density can be tuned in a highly programmable way. The modified surfaces are selectively responsive towards complementary analytes, thus allowing accurate kinetic and thermodynamic information to be obtained.