Selective recognition of biologically relevant proteins is a growing topic of interest as it pertains to the medical and pharmaceutical industry. As a step toward the goal of selective protein recognition, we have been studying the binding of acyclic cucurbiturils with amino acid amides by 1H NMR and Isothermal Titration Calorimetry (ITC). Our initial results show that acyclic Cucurbiturils, Motor 1 and Motor 2, have high affinity toward phenylalanine amide (Ka= 3.24 x 106 M-1 for Phe) which is the N-terminal residue of insulin which suggests its application in protein recognition. This is higher compared to other molecular containers such as macrocyclic CB[7] (Ka= 1.8 x 106 M-1 for Phe). We present the results of our 1H NMR and ITC binding studies of several acyclic CB[n] type containers toward the 19 amino acid amides.

Molecular recognition of amino acid amides by acyclic cucurbiturils

254th National Meeting (2017)

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