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The MMP enzyme cleaves the peptide covalently attached to the 129Xe biosensor, resulting in a change in the chemical environment of 129Xe readily detectable by a 0.5 ppm chemical shift in NMR. The features of these tri-functionalized cryptophanes enable the detection of picomolar concentrations of cryptophane biosensors by a technique known as Hyper-CEST NMR/MRI. Additional xenon biosensors have been designed to target integrin receptors, folate receptor, and carbonic anhydrase. In most cases, binding the cryptophane biosensor to its protein target produces a measureable change in the Xe-129 NMR chemical shift.