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Folding of a salivary intrinsically disordered protein upon binding to tannins

Francis Canon1, Renaud Ballivian, Fabien Chirot

  • 1INRA, UMR1083 Science Pour l'Oenologie, Polyphenol Interaction, Bât 28, 2 place Viala F-34060 Montpellier, France.

Journal of the American Chemical Society
|April 29, 2011
PubMed

We used ion mobility spectrometry to explore conformational adaptability of intrinsically disordered proteins bound to their targets in complex mixtures. We investigated the interactions between a human salivary proline-rich protein IB5 and a model of wine and tea tannin: epigallocatechin gallate (EgCG). Collisional cross sections of naked IB5 and IB5 complexed with N = 1-15 tannins were recorded. The data demonstrate that IB5 undergoes an unfolded to folded structural transition upon binding with EgCG.

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