Peptide conformational changes induced by tryptophan–phosphocholine interactions in a micelle
- 10 October 2002
- journal article
- research article
- Published by Wiley in Biopolymers
- Vol. 65 (5), 354-361
- https://doi.org/10.1002/bip.10272
Abstract
Sodium dodecylsulfate (SDS) and dodecylphosphocholine (DPC) micelles are often used to mimic the membrane- or receptor-bound states of peptides in NMR studies. From the present examination of a 26-residue analog of exendin-4 (TrEX4) by NMR and CD in water, aqueous 30% trifluoroethanol (TFE), and bound to both SDS and DPC micelles, it is clear that these two lipid micelles can yield very different peptide structures. The Trp-cage fold (also observed in 30% TFE) is present when TrEX4 is bound to SDS micelles; however, tertiary structure is absent in the presence of DPC micelles. The loss of tertiary structure is attributed to an energetically favorable interaction (estimated as 2–3 kcal/mol) of the tryptophan side chain with the phosphocholine head groups. These dramatic structural differences suggest that care must be taken when using either SDS or DPC to mimic the membrane- or receptor-bound states. © 2002 Wiley Periodicals, Inc. Biopolymers 65: 354–361, 2002Keywords
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