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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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Yèagle, P. L. (2013) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2013.11.009 · Cited by 157
“If however the protein is in a bilayer that is thinner than the hydrophobic surface on the protein, the protein may alter conformation (such as a tilt [1–3] or a bend [4,5] in the transmembrane portion) to better accommodate the hydrophobic portion of the bilayer, or the bilayer may distort to cover the hydrophobic su…”
BackgroundFabiani, C., & Antollini, S. S. (2019) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00309 · Cited by 158
“Contrarily, non-annular lipids are in close contact with the protein, probably in between α-helix transmembrane segments or subunits, and can be associated to lipid binding sites with a slow exchange rate with bulk lipids (Lee, 2003).”
BackgroundExploring the membrane proteome—Challenges and analytical strategies
Helbig, A. O., Heck, A. J. R., & Slijper, M. (2010) · Journal of Proteomics · doi:10.1016/j.jprot.2010.01.005 · Cited by 154
“show crucial impact on the function of membrane proteins [64].”
BackgroundSynthetic peptides as models for intrinsic membrane proteins
Killian, J. A. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)01154-2 · Cited by 152
Docosahexaenoic acid alters bilayer elastic properties
Bruno, M. J., Koeppe, R. E., & Andersen, O. S. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701015104 · Cited by 150
Angelov, B., Angelova, A., Filippov, S. K., Drechsler, M., Štěpánek, P., & Lesieur, S. (2014) · ACS Nano · doi:10.1021/nn5012946 · Cited by 151
Adaptation of the membrane in Archaea
Oger, P., & Cario, A. (2013) · Biophysical Chemistry · doi:10.1016/j.bpc.2013.06.020 · Cited by 149
“As can be expected from the central role of the membrane for the cell, perturbation in lipid phase state has profound consequences on membrane structure and function [41,42].”
TMDET: web server for detecting transmembrane regions of proteins by using their 3D coordinates
Tusnády, G., Dosztányi, Z., & Simon, I. (2004) · Bioinformatics · doi:10.1093/bioinformatics/bti121 · Cited by 149
“With the exception of a few tightly bound lipid molecules, the deposited experimental data have no direct indication that the protein is immersed into the membrane under native conditions, and do not contain information about the exact location of the lipid bilayer (Lee, 2003).”
BackgroundSpin Selectivity in Photoinduced Charge-Transfer Mediated by Chiral Molecules
Abendroth, J. M., Stemer, D. M., Bloom, B. P., Roy, P., Naaman, R., Waldeck, D. H., Weiss, P. S., & Mondal, P. C. (2019) · ACS Nano · doi:10.1021/acsnano.9b01876 · Cited by 150
Specific protein–lipid interactions in membrane proteins
Hunte, C. (2005) · Biochemical Society Transactions · doi:10.1042/bst20050938 · Cited by 145
Control of the postsynaptic membrane viscosity
Renner, M., Choquet, D., & Triller, A. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.4445-08.2009 · Cited by 145
“The rigidity of lipids that surround integral proteins is strongly affected by the protein (Anderson and Jacobson, 2002; Lee, 2003).”
BackgroundLipids from Hermetia illucens, an Innovative and Sustainable Source
Franco, A., Scieuzo, C., Salvia, R., Petrone, A. M., Tafi, E., Moretta, A., Schmitt, É., & Falabella, P. (2021) · Sustainability · doi:10.3390/su131810198 · Cited by 170
Screening Blockers Against a Potassium Channel with a Droplet Interface Bilayer Array
Syeda, R., Holden, M. A., Hwang, W. L., & Bayley, H. (2008) · Journal of the American Chemical Society · doi:10.1021/ja804968g · Cited by 142
Identification of Cholesterol Binding Sites in the Serotonin1A Receptor
Sengupta, D., & Chattopadhyay, A. (2012) · The Journal of Physical Chemistry B · doi:10.1021/jp309888u · Cited by 141
Swainsbury, D. J. K., Scheidelaar, S., van Grondelle, R., Killian, J. A., & Jones, M. R. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201406412 · Cited by 138
Lipids in photosynthetic reaction centres: Structural roles and functional holes
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Interactions between lipids and voltage sensor paddles detected with tarantula toxins
Milescu, M., Bosmans, F., Lee, S., Alabi, A. A., Kim, J. I., & Swartz, K. J. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1679 · Cited by 137
“1, the effects of modification of sphingomyelin can be diminished by toxins that bind to voltage sensors 7, raising the possibility that sphingomyelin interacts directly with voltage sensors in the channel, perhaps similar to the non-annular lipids observed for other membrane proteins 13,14.”
Marius, P., Zagnoni, M., Sandison, M. E., et al. (2007) · Biophysical Journal · doi:10.1529/biophysj.107.117507 · Cited by 135
“In studies of lipid binding, it is convenient to distinguish between two classes of site, annular or boundary sites on the transmembrane surface of a membrane protein, and nonannular sites located between transmembrane a-helices (9,10); according to this definition, the lipid binding sites identified in the crystal st…”
BackgroundSelf-citationFlotillins functionally organize the bacterial membrane
Bach, J. N., & Bramkamp, M. (2013) · Molecular Microbiology · doi:10.1111/mmi.12252 · Cited by 137
“of membrane embedded protein machineries such as the protein secretion system need a specialized lipid environment (Lee, 2003).”
BackgroundInfluentialPrinciples of membrane protein interactions with annular lipids deduced from aquaporin‐0 2D crystals
Hite, R. K., Li, Z., & Walz, T. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.68 · Cited by 134
“Together, these observations suggest that the exact chemical identities of the phospholipid headgroups have a negligible role in the interaction of annular lipids with membrane proteins, corroborating previous results obtained by spin-labelling studies (Lee, 2003).”
BackgroundResultCharacterization of Two Oxidatively Modified Phospholipids in Mixed Monolayers with DPPC
Sabatini, K., Mattila, J.-P., Megli, F. M., & Kinnunen, P. K. J. (2006) · Biophysical Journal · doi:10.1529/biophysj.105.080176 · Cited by 126
Bagos, P. G., Liakopoulos, T. D., & Hamodrakas, S. J. (2005) · BMC Bioinformatics · doi:10.1186/1471-2105-6-7 · Cited by 126
“Thus, it is believed that the outer membrane possesses an average thickness around 25–30 Å, a fact mainly explainable by its lipid composition, average hydrophobicity and asymmetry [51].”
How lipids and proteins interact in a membrane: a molecular approach
LEE, A. G. J. (2005) · Molecular BioSystems · doi:10.1039/b504527d · Cited by 125
Self-citationInteraction of Melittin with Membrane Cholesterol: A Fluorescence Approach
Raghuraman, H., & Chattopadhyay, A. (2004) · Biophysical Journal · doi:10.1529/biophysj.104.043596 · Cited by 125
“Lipid-protein interactions are vital for the organization and function of biological membranes (Lee, 2003).”
BackgroundA subset of annular lipids is linked to the flippase activity of an ABC transporter
Bechara, C., Noll, A., Morgner, N., Degiacomi, M. T., Tampé, R., & Robinson, C. V. (2015) · Nature Chemistry · doi:10.1038/nchem.2172 · Cited by 130
Coarse-grained simulation: a high-throughput computational approach to membrane proteins
Sansom, M. S. P., Scott, K. A., & Bond, P. J. (2008) · Biochemical Society Transactions · doi:10.1042/bst0360027 · Cited by 122
Seigneuret, M. (2005) · Biophysical Journal · doi:10.1529/biophysj.105.069666 · Cited by 122
“Complete spanning of the lipid bilayer (;40 Å) by a transmembrane helix requires an at least 26-residue length (42).”
BackgroundInsights on P-Glycoprotein’s Efflux Mechanism Obtained by Molecular Dynamics Simulations
Ferreira, R. J., Ferreira, M. U., & dos Santos, D. J. V. A. (2012) · Journal of Chemical Theory and Computation · doi:10.1021/ct300083m · Cited by 123
Conn, C. E., & Drummond, C. J. (2013) · Soft Matter · doi:10.1039/c3sm27743g · Cited by 120
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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