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Hydrophobic interactions of peptides with membrane interfaces
Open accessAbstract
The thermodynamic principles underlying the structural stability of membrane proteins are difficult to obtain directly from whole proteins because of intractable problems related to insolubility in the aqueous phase and extreme stability in the membrane phase. The principles must therefore be surmised from studies of the interactions of small peptides with lipid bilayers. This review is concerned with the hydrophobic interactions of such peptides with the interfacial regions of lipid bilayers. We first develop a general framework for thinking about the thermodynamics of membrane protein stability that centers on interfacial interactions and review the structural and chemical evidence that supports this interface-centered point of view. We then describe an experimentally determined whole-residue interfacial hydrophobicity scale that reveals the central role of the peptide bond in partitioning and folding. Finally, we consider the complexity and diversity of interfacial interactions revealed by differences between side-chain hydrophobicities determined using different classes of peptides.
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Citations
Cited by
MEMBRANE PROTEIN FOLDING AND STABILITY: Physical Principles
White, S. H., & Wimley, W. C. (1999) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.28.1.319 · Cited by 1,764
Self-citationPrebiotic Peptides: Molecular Hubs in the Origin of Life
Frenkel-Pinter, M., Samanta, M., Ashkenasy, G., & Leman, L. J. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00664 · Cited by 354
Lipid vesicles as possible intermediates in the origin of life
Luisi, P. L., Walde, P., & Oberholzer, T. (1999) · Current Opinion in Colloid & Interface Science · doi:10.1016/s1359-0294(99)00012-6 · Cited by 287
Role of molecular charge and hydrophilicity in regulating the kinetics of crystal growth
Elhadj, S., De Yoreo, J. J., Hoyer, J. R., & Dove, P. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0605748103 · Cited by 270
The Secretion and Action of Brush Border Enzymes in the Mammalian Small Intestine
Hooton, D., Lentle, R., Monro, J., Wickham, M., & Simpson, R. (2015) · Reviews of Physiology, Biochemistry and Pharmacology · doi:10.1007/112_2015_24 · Cited by 145
Metadata
- Authors
- White, S. H., & Wimley, W. C.
- Venue
- Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes
- Publisher
- Elsevier BV
- Published
- 1998-11
- Volume
- 1376
- Issue
- 3
- Pages
- 339-352
- ISSN
- 0304-4157 (ISSN-L)
- OpenAlex
- W2000729091
- Cited by
- 556
- References
- 0
- FWCI
- 7.32
- Type
- journal article
- Language
- en
- Open access
- green
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- White, S. H., & Wimley, W. C. (1998). Hydrophobic interactions of peptides with membrane interfaces. Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes. https://doi.org/10.1016/s0304-4157(98)00021-5
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
