Using surface plasmon resonance to directly identify molecules in a tripeptide library that bind tightly to a vancomycin chip.
This paper describes a procedure, based on direct binding, for identifying tight-binding ligands for a receptor immobilized on a sensor chip from an array of equimolar tripeptides using surface plasmon resonance. Vancomycin and a library of 96 tripeptides, with molecular weight ranging from 316 to 560 Da, were used as a model system to illustrate the procedure. A consensus structure of the strongest interacting peptides consisted of D-Ala at the C terminus and aromatic amino acid in the penultimate position. Ligands having this structure bound more tightly to vancomycin than the known D-Ala-D-Ala peptide. The throughput of our continuous assay is 96 compounds in 3.3 h, and the sample consumption is less than 2 microg per peptide and 1 ng for vancomycin. This procedure should be applicable to peptide libraries of greater complexity than that used here and to mixtures of small organic compounds.
Tseng
Ming-Chung
MC
Department of Chemistry and Biochemistry, National Chung Cheng University, Chia-Yi, Taiwan 621, Taiwan, ROC.
Chu
Yen-Ho
YH
D008024:Ligands; D019151:Peptide Library; D010455:Peptides / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D020349:Surface Plasmon Resonance / Q000379:methods*; D014640:Vancomycin / Q000378:metabolism*
D008024:Ligands; D019151:Peptide Library; D010455:Peptides; D014640:Vancomycin