Abstract
The interaction of cyclodextrins (CDs) with poly(N-methacryloyltryptophan) (pMTrp) and with poly(N-methacryloylphenylalanine) (pMPhe) was investigated as a simple model system of macromolecular recognition of proteins. The association constants (K) for the model compounds, sodium salts of tryptophan and phenylalanine, are not so different (i.e. 43 and 16M−1 for α-CD, 59 and 69M−1 for β-CD, and 12 and 3M−1 for γ-CD, respectively). On the other hand, there is a significant difference in the apparent K values for pMTrp and pMPhe (i.e. the K values for pMPhe are considerably smaller than ca. 10M−1, whereas those for pMTrp are 30, 83, and 11M−1 for α-, β-, and γ-CDs, respectively). These observations indicate that a subtle difference in polymer side chains can be critical in macromolecular recognition.
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