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Lipid–protein interactions in biological membranes: a structural perspective
Open accessAbstract
Lipid molecules bound to membrane proteins are resolved in some high-resolution structures of membrane proteins. An analysis of these structures provides a framework within which to analyse the nature of lipid-protein interactions within membranes. Membrane proteins are surrounded by a shell or annulus of lipid molecules, equivalent to the solvent layer surrounding a water-soluble protein. The lipid bilayer extends right up to the membrane protein, with a uniform thickness around the protein. The surface of a membrane protein contains many shallow grooves and protrusions to which the fatty acyl chains of the surrounding lipids conform to provide tight packing into the membrane. An individual lipid molecule will remain in the annular shell around a protein for only a short period of time. Binding to the annular shell shows relatively little structural specificity. As well as the annular lipid, there is evidence for other lipid molecules bound between the transmembrane alpha-helices of the protein; these lipids are referred to as non-annular lipids. The average thickness of the hydrophobic domain of a membrane protein is about 29 A, with a few proteins having significantly smaller or greater thicknesses than the average. Hydrophobic mismatch between a membrane protein and the surrounding lipid bilayer generally leads to only small changes in membrane thickness. Possible adaptations in the protein to minimise mismatch include tilting of the helices and rotation of side chains at the ends of the helices. Packing of transmembrane alpha-helices is dependent on the chain length of the surrounding phospholipids. The function of membrane proteins is dependent on the thickness of the surrounding lipid bilayer, sometimes on the presence of specific, usually anionic, phospholipids, and sometimes on the phase of the phospholipid.
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“Fatty acyl chain length alters binding constants of several membrane proteins [169], making it tempting to speculate that VLCFAs might alter neural cell membrane structure, stability, and function [170].”
From Revisiting the Pathogenesis of X-Linked Adrenoleukodystrophy (2025) · cites this paper as [169]
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Membrane Thickness Changes Ion-Selectivity of Channel-Proteins
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Fišar, Z., Anders, M., TVRZICKÁ, E., & Staňková, B. (2005) · PubMed · Cited by 19
Roszak, A. W., Gardiner, A. T., Isaacs, N. W., & Cogdell, R. J. (2007) · Biochemistry · doi:10.1021/bi062154i · Cited by 19
Interaction of Serotonin1A Receptors from Bovine Hippocampus with Tertiary Amine Local Anesthetics
Kalipatnapu, S., & Chattopadhyay, A. (2004) · Cellular and Molecular Neurobiology · doi:10.1023/b:cemn.0000022771.33702.85 · Cited by 19
“These results are difficult to interpret in view of the significance of lipid–protein interactions in the functioning of membrane proteins (Lee, 2003) and the sensitivity of the ligand-binding properties of the bovine hippocampal 5-HT1A receptor to membrane cholesterol content itself (Pucadyil, T.”
BackgroundJayasekera, H. S., Mohona, F. A., Ewbank, M. A., & Marty, M. T. (2024) · Analytical Chemistry · doi:10.1021/acs.analchem.4c01704 · Cited by 18
Effects of lipid environment on the conformational changes of an ABC importer
Rice, A. J., Alvarez, F. J. D., Davidson, A. L., & Pinkett, H. W. (2014) · Channels · doi:10.4161/chan.29294 · Cited by 18
“It is important to understand how these membrane-embedded proteins interact with the lipid molecules found in their natural environment.(2) Transmembrane (TM) proteins insert into the lipid bilayer allowing for the non-polar regions to contact the hydrophobic lipid tails and polar regions to be exposed to the aqueous…”
BackgroundA concise method for quantitative analysis of interactions between lipids and membrane proteins
Inada, M., Kinoshita, M., Sumino, A., et al. (2019) · Analytica Chimica Acta · doi:10.1016/j.aca.2019.01.042 · Cited by 18
Furse, S., Fernandez‐Twinn, D. S., Beeson, J. H., Chiarugi, D., Ozanne, S. E., & Koulman, A. (2022) · Nutrition and Diabetes · doi:10.1038/s41387-022-00185-4 · Cited by 19
“The relationship between membrane composition and membrane protein activity is well established [58, 59].”
BackgroundHydrophobic Mismatch in Membranes: When the Tail Matters
Rao, B. D., Shrivastava, S. K., & Chattopadhyay, A. (2017) · Springer series in biophysics · doi:10.1007/978-3-319-66601-3_16 · Cited by 18
“Hydrophobic thickness may be determined directly from crystal structures when the structure contains resolved lipid molecules that would mark the membrane interface [23].”
BackgroundKinetics of Histidine-Tagged Protein Association to Nickel-Decorated Liposome Surfaces
Raghunath, G., & Dyer, R. B. (2019) · Langmuir · doi:10.1021/acs.langmuir.9b01700 · Cited by 18
Darling, L. E. O., & Raphael, R. M. (2009) · Journal of the Association for Research in Otolaryngology · doi:10.1007/s10162-009-0171-1 · Cited by 18
“…through changes in the hydrophobic bilayer thickness, membrane curvature, lipid packing density, and the lateral pressure profile (Yeagle 1991; Cantor 1999; Lee 2003; Jensen and Mouritsen 2004; Mouritsen and Zuckermann 2004; McIntosh and Simon 2006; Andersen and Koeppe 2007; Niemela et al. 2007).”
BackgroundLipid dependence and activity control of phosphatidylserine synthase from Escherichia coli
Linde, K., Gröbner, G., & Rilfors, L. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.08.038 · Cited by 18
Kong, L., Dawkins, E., Campbell, F., Winkler, E., Derks, R. J. E., Giera, M. A., Kamp, F., Steiner, H., & Kros, A. (2020) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2020.183200 · Cited by 17
“Thus, the activity of ion channels, transporters and membrane-associated enzymes have all been shown sensitive to changes in lipid membrane composition [10–13].”
BackgroundIdentifying lipids tightly bound to an integral membrane protein
de Vlugt, J., Xiao, P., Munro, R. A., et al. (2020) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2020.183345 · Cited by 17
Morzy, D., Joshi, H., Sandler, S. E., et al. (2021) · Nano Letters · doi:10.1021/acs.nanolett.1c03791 · Cited by 17
Resonance energy transfer study of lysozyme–lipid interactions
Gorbenko, G. P., Ioffe, V. M., Molotkovsky, J. G., et al. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.09.027 · Cited by 17
“This finding supports the notion that tryptophan residues of membrane-bound peptides and proteins tend to reside at lipid–water interface [3,35].”
ResultTsuda, K. (2010) · Journal of Obesity · doi:10.1155/2011/548140 · Cited by 17
“However, the influence of adiponectin on the membrane lipid-protein interactions [35, 36] cannot be fully excluded.”
BackgroundThe Carnitine Transporter Network: Interactions with Drugs
Indiveri, C., Pochini, L., Oppedisano, F., & Tonazzi, A. (2010) · Current Chemical Biology · doi:10.2174/2212796811004020108 · Cited by 17
“3) which has been constructed on the basis of hydropathy analysis for membrane proteins [43, 86] and the experimental data.”
BackgroundPostic, G., Ghouzam, Y., Guiraud, V., & Gelly, J. (2015) · Protein Engineering Design and Selection · doi:10.1093/protein/gzv063 · Cited by 17
“Despite the possibility of manually assigning the lipid bilayer boundaries (Lee, 2003), the size of the current datasets of membrane protein structures (e.g. the 15340 models from EVfold_membrane (Hopf et al., 2012)), requires the use of automated methods.”
MethodMembrane Curvature Affects the Formation of α-Hemolysin Nanopores
Fujii, S., Matsuura, T., & Yomo, T. (2015) · ACS Chemical Biology · doi:10.1021/acschembio.5b00107 · Cited by 17
Structural Dynamics of the Paddle Motif Loop in the Activated Conformation of KvAP Voltage Sensor
Das, A., Chatterjee, S., & Raghuraman, H. (2019) · Biophysical Journal · doi:10.1016/j.bpj.2019.08.017 · Cited by 17
“Membrane lipids play an important role in modulating the structure and function of various membrane proteins particularly because of their specific high-affinity binding (57,58).”
BackgroundSukumaran, S., Hauser, K., Rauscher, A., et al. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.03.059 · Cited by 17
“resulting in a thickness of 24–28 Å for the hydrophobic core of the protein (for a review see [4]).”
BackgroundPantano, D. A., & Klein, M. L. (2009) · The Journal of Physical Chemistry B · doi:10.1021/jp901840u · Cited by 17
Nanoscale patterning controls inorganic–membrane interface structure
Almquist, B. D., Verma, P., Wei Cai, A., et al. (2010) · Nanoscale · doi:10.1039/c0nr00486c · Cited by 17
Potential role of the membrane in hERG channel functioning and drug-induced long QT syndrome
Chartrand, É., Arnold, A. A., Gravel, A. E., et al. (2010) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2010.05.019 · Cited by 17
Assessing the Role of Lipids in the Molecular Mechanism of Membrane Proteins
Jodaitis, L., van Oene, T., & Martens, C. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22147267 · Cited by 20
Metadata
- Authors
- Lee, A. G.
- Affiliations
- University of Southampton (GB)
- Corresponding author
- Lee, A.G
- Venue
- Biochimica et Biophysica Acta (BBA) - Biomembranes
- Publisher
- Elsevier BV
- Published
- 2003-05
- Volume
- 1612
- Issue
- 1
- Pages
- 1-40
- ISSN
- 0005-2736 (ISSN-L)
- OpenAlex
- W2128882835
- Cited by
- 886
- References
- 224
- Citations by year
- 2026: 31 · 2025: 30 · 2024: 25 · 2023: 16 · 2022: 32 · 2021: 33 · 2020: 31 · 2019: 51 · 2018: 37 · 2017: 33 · 2016: 32 · 2015: 51 · 2014: 47 · 2013: 38 · 2012: 32
- FWCI
- 3.71
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biochimica et Biophysica Acta (BBA) - Biomembranes (publishedVersion)
- PubMed (publishedVersion)
- ePrints Soton (University of Southampton) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Keywords
- protein-lipid interactions, membrane proteins, lipid bilayers, transmembrane helices, hydrophobic mismatch, membrane thickness, helix tilt, anionic phospholipids, lipid phase, membrane protein structure
- MeSH terms
- Animals, Bacteriorhodopsins, Crystallization, Humans, Lipid Bilayers, Membrane Lipids, Membrane Proteins, Protein Structure, Secondary, Photosynthetic Reaction Center Complex Proteins, Hydrophobic and Hydrophilic Interactions
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