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An array sensing scheme for the differentiation of small peptides and their phosphorylated analogues is introduced. The technique involves a series of receptors created by appending random peptides to a C(3v) symmetric scaffold that binds phosphomonoesters. Five specific peptide sequences were selected through a screening technique. In addition to cross reactivity being created by the peptides in the receptors, three metal ions and three pH indicators are used to create a suite of 45 indicator displacement assays. The colorimetric data from the 45 sensing ensembles is collected in a 96-well plate reader, and linear discriminant analysis gives patterns resulting in 100% classification of the peptides. The approach demonstrates a generalizable principle to create pattern-based recognition protocols for complex analytes.
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Zhang et al. (2009) studied this question.
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