Tannin interactions with a full‐length human salivary proline‐rich protein display a stronger affinity than with single proline‐rich repeats

FEBS Letters

Lilley, Terence H.¹  Haslam, Edwin¹  McDonald, Charles J.²  Baxter, Nicola J.²  Charlton, Adrian J.²  Williamson, Michael P.² 

[1] Department of Chemistry, The Krebs Institute for Biomolecular Research, University of Sheffield, Sheffield S3 7HF, UK;Department of Molecular Biology and Biotechnology, The Krebs Institute for Biomolecular Research, University of Sheffield, Sheffield S10 2UH, UK

关键词: 1H-NMR;    Tannin;    Salivary proline-rich protein;    Intramolecular binding;    Hydrophobic interaction;   

DOI  :  10.1016/0014-5793(96)00186-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The protein IB5 has been purified from human parotid saliva. This protein contains several repeats of a short proline-rich sequence. Dissociation constants have been measured at several discrete binding sites using ¹H-NMR for the hydrolysable tannins (polyphenols) (, and and the condensed proanthocyanidin (−)-epicatechin. The dissociation constants for trigalloyl glucose and pentagalloyl glucose were 15 × 10⁻⁵ and 1.7 × 10⁻⁵ M, respectively, which are 115 and 1660 times stronger than those previously measured under the same conditions for a single repeat of a mouse salivary proline-rich protein. The increase in affinity is ascribed to intramolecular secondary interactions, which are strengthened by the rigidity of the interacting molecules.

【 授权许可】

Unknown