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Investigation of the stereoselectivity of an anti-amino acid antibody utilizing tryptophan fluorescence
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The binding sites of proteins such as antibodies are known to often contain tryptophan (Trp) residues, whose fluorescent properties may be altered upon ligand binding. Conformational changes within the binding site or simply the presence of the ligand can result in either fluorescence quenching or enhancement, which may be utilized to quantitatively investigate protein-ligand interactions. We have previously described the production of highly stereoselective antibodies to amino acids. These antibodies have been used in a variety of analytical techniques for the sensitive detection of enantiomeric impurities and for enantiomer separation. The objective of this study was to test if tryptophan fluorescence can be used to determine the affinity of an anti-D-amino acid antibody toward a variety of standard and non-standard amino acids. In order to examine the utility of BMG LABTECH’s FLUOstar for measuring Trp fluorescence, experimental conditions were first optimized using the free amino acid as analyte.

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