NOE studies on the complexation of (poly) flavanoids with peptides containing proline residues in aqueous solutions reveal site specific approach directed by hydrophobic interaction of the aromatic rings of catechin and its dimer, catechin-(4α→ 8)-catechin, to conformationally accessible regions of peptides without strong preference for interaction with proline residues.
T. Hatano and R. W. Hemingway, Chem. Commun., 1996, 2537 DOI: 10.1039/CC9960002537
To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.
If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.
If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.
Read more about how to correctly acknowledge RSC content.
Please wait while we load your content...
