Cited by 886Lipid Membrane Structure and BehaviorProtein Structure and DynamicsReceptor Mechanisms and Signaling

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Lipid–protein interactions in biological membranes: a structural perspective

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Lee, A.G·2003·Biochimica et Biophysica Acta (BBA) - Biomembranes

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Abstract

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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Capability of ganglioside GM1 in modulating interactions, structure, location and dynamics of peptides/proteins: biophysical approaches
Khatun, U. L., Gayen, A., & Mukhopadhyay, C. (2014) · Glycoconjugate Journal · doi:10.1007/s10719-014-9554-6 · Cited by 5
“Fluorescence spectroscopy is amongst the most widely used techniques for studying lipid–protein interactions due to the intrinsic sensitivity, suitable timescale and minimal perturbation [46–48].”
BackgroundMethod
Membrane Interface Composition Drives the Structure and the Tilt of the Single Transmembrane Helix Protein PMP1: MD Studies
Beswick, V., Isvoran, A., Nédellec, P., et al. (2011) · Biophysical Journal · doi:10.1016/j.bpj.2011.02.002 · Cited by 5
Over‐expression of the Anti‐apoptotic Protein Bcl‐2 Affects Membrane Lipid Composition in HL‐60 Cells
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Specific volume and compressibility of bilayer lipid membranes with incorporated Na,K-ATPase
Hianik, T., Rybár, P., Krivánek, R., et al. (2011) · General Physiology and Biophysics · doi:10.4149/gpb_2011_02_145 · Cited by 5
Causes, Mechanisms and Prevention of Environmental Diseases
Zeliger, H. I. (2016) · Dual Diagnosis Open Access · doi:10.21767/2472-5048.100001 · Cited by 5
“86 Park SJ, Lee JH, Woo SJ, Kang SW, Park KH (2015) Epidemiologic Survey Committee of Korean Ophthalmologic Society Five heavy metallic elements and age-related macular degeneration: Korean National Health and Nutrition Examination Survey, 2008-2011.”
BackgroundInfluential
Lipid nanotechnologies for structural studies of membrane-associated clotting proteins by cryo-electron microscopy
Stoilova‐McPhie, S. (2016) · Nanotechnology Reviews · doi:10.1515/ntrev-2016-0066 · Cited by 5
Kinetics of Domain Formation Processes in Lipid Membranes
Seeger, H. M. (2006) · doi:10.53846/goediss-2777 · Cited by 5
Structural Biology of Membrane Proteins
Salom, D., & Palczewski, K. (2011) · Wiley eBooks · doi:10.1002/9783527634521.ch9 · Cited by 5
A combined lipidomic and proteomic profiling of Arabidopsis thaliana plasma membranePreprint
Bahammou, D., Recorbet, G., Cassim, A. M., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.05.14.540643 · Cited by 5
Hermetia illucens as an innovative feedstock for biodiesel: properties, production techniques, and regulatory compliance
Pucciarelli, V., Ianniciello, D., Schmitt, É., Scieuzo, C., & Falabella, P. (2026) · Bioresource Technology · doi:10.1016/j.biortech.2026.134016 · Cited by 4
Vinyl ether maleic acid block copolymers: a versatile platform for tunable self-assembled lipid nanodiscs and membrane protein characterization
Shah, M. Z., Okorafor, E. A., Rotich, N. C., Henoch, Q., Acharya, R. T., Page, R. C., Lorigan, G. A., & Konkolewicz, D. (2025) · Polymer Chemistry · doi:10.1039/d5py00767d · Cited by 4
Functional analysis of phosphoethanolamine N-methyltransferase in plants and parasites: Essential S-adenosylmethionine-dependent methyltransferase in choline and phospholipid metabolism
Bare, A., Thomas, J., Etoroma, D., et al. (2022) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2022.08.028 · Cited by 4
Humidity-Responsive Polymer Cushion-Supported Biomimetic Membrane: A Model System for X-ray Studies
Giri, R. P., & Mukhopadhyay, M. K. (2022) · Langmuir · doi:10.1021/acs.langmuir.2c02533 · Cited by 4
The impact of transmembrane peptides on lipid bilayer structure and mechanics: A study of the transmembrane domain of the influenza A virus M2 protein
Gamage, Y. I., Wadumesthri, Y. M., Gutiérrez, H. R., et al. (2024) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2024.184373 · Cited by 4
Effect of Simulated Microgravity on Artificial Single Cell Membrane Mechanics
Prabu, R., Manohar, A., Narendran, S., et al. (2024) · Microgravity Science and Technology · doi:10.1007/s12217-024-10133-9 · Cited by 4
“In DPH-labeled systems, we can obtain the microviscosity by simply measuring �uorescence polarization, using Shinitzky's equation (Lee, 2003) for the approximate evaluation of Fluorescent depolarization is caused by the rotational diffusion of �uorophores, which corresponds to the diffusivity of…”
5.12 Membrane Protein–Lipid Match and Mismatch
Mouritsen, O. G. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-374920-8.00521-x · Cited by 4
Membrane lipids and proteins as modulators of urothelial endocytic vesicles pathways
Grasso, E. J., & Calderón, R. O. (2013) · Histochemistry and Cell Biology · doi:10.1007/s00418-013-1095-8 · Cited by 4
Protein–Lipid Interactions in the Brain
Fantini, J., & Yahi, N. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-800111-0.00006-0 · Cited by 4
Single-Molecule Fluorescence Studies of Membrane Transporters Using Total Internal Reflection Microscopy
Goudsmits, J. M. H., van Oijen, A. M., & Slotboom, D. J. (2017) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2017.05.009 · Cited by 4
“At the same time, membrane proteins interact with the surrounding lipids (Lee, 2003; Marsh, 2008), affecting protein folding and functioning (Lee, 2004; Phillips, Ursell, Wiggins, & Sens, 2009).”
Background
The Effects of Calcium on Lipid–Protein Interactions and Ion Flux in the Cx26 Connexon Embedded into a POPC Bilayer
Albano, J. M. R., Jara, G. E., Fernández, M. L., et al. (2019) · The Journal of Membrane Biology · doi:10.1007/s00232-019-00088-z · Cited by 4
Fluorescence Resonance Energy Transfer (FRET) as a Spectroscopic Ruler for the Investigation of Protein Induced Lipid Membrane Curvature: Bacteriorhodopsin and Bacteriorhodopsin Analogs in Model Lipid Membranes
Bryl, K. (2022) · Applied Spectroscopy · doi:10.1177/00037028221135645 · Cited by 4
Structural mass spectrometry approaches to understand multidrug efflux systems
Lewis, B. R., Lawrence, R., Hammerschmid, D., & Reading, E. (2022) · Essays in Biochemistry · doi:10.1042/ebc20220190 · Cited by 4
“Lipids are essential for the function of membrane proteins; the phase/presence of particular phospholipids has an effect, as does the thickness of the surrounding bilayer [61].”
Coarse-grained methods for heterogeneous vesicles with phase-separated domains: Elastic mechanics of shape fluctuations, plate compression, and channel insertion
Rower, D. A., & Atzberger, P. J. (2023) · Mathematics and Computers in Simulation · doi:10.1016/j.matcom.2023.02.020 · Cited by 4
“This includes the insertion, assembly, and activation of membraneproteins such as channels, receptors, or anchoring sites of the cytoskeleton [3, 9, 10, 11, 12].”
Background
Anionic Phospholipids Shift the Conformational Equilibrium of the Selectivity Filter in the KcsA Channel to the Conductive Conformation: Predicted Consequences on Inactivation
Renart, M. L., Giudici, A. M., Coll-Díez, C., et al. (2023) · Biomedicines · doi:10.3390/biomedicines11051376 · Cited by 4
“The crystallographic evidence and other studies [43] conclude that the PG binding sites on the KcsA protein have the features of so-called “non-annular” lipid binding sites on the protein surface [44] between the TM1 and TM2 of each pair of adjacent KcsA monomers.”
Background
The Influence of Fatty Acids on the GpA Dimer Interface by Coarse-Grained Molecular Dynamics Simulation
Flinner, N., Mirus, O., & Schleiff, E. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms150814247 · Cited by 4
“This results from the enhanced number of possible van der Waals contacts [10], independently of the hydrophobic thickness of the different phases [11].”
Interactions between Polymers and Phospholipid Membranes
Liu, G., & Zhang, G. (2013) · Springer briefs in molecular science · doi:10.1007/978-3-642-39790-5_5 · Cited by 4
Greasing the gears of potassium channels
Swartz, K. J. (2006) · Nature Chemical Biology · doi:10.1038/nchembio0806-401 · Cited by 4
Modulating Inhibitory Ligand-Gated Ion Channels
Cascio, M. G. (2006) · The AAPS Journal · doi:10.1208/aapsj080240 · Cited by 4
Transmembrane Domains in Membrane Protein Folding, Oligomerization, and Function
Ridder, A. N. J. A., & Langosch, D. (2005) · doi:10.1002/9783527619498.ch59 · Cited by 4
Biological and Biomimetic Membranes
Kumar, M., Shen, Y., & Saboe, P. O. (2013) · doi:10.1002/9781118522318.emst051 · Cited by 4
Cell division in Escherichia coli
Skoog, K. (2011) · KTH Publication Database DiVA (KTH Royal Institute of Technology) · Cited by 4
Implications for OLE RNA as a natural integral membrane RNA
Lyon, S. E., & Breaker, R. R. (2025) · RNA · doi:10.1261/rna.080489.125 · Cited by 3
“The glycerol-to-glycerol distance of a typical phospholipid bilayer is ∼ 35 Å (Lee 2003).”
Membrane properties control the ATPase activity of the ABC transporter BmrA
Osten, V., & Schneider, D. (2025) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2025.184430 · Cited by 3
Towards sustainable lipidomics: computational screening and experimental validation of chloroform-free alternatives for lipid extraction
Venturi, A., Wölk, M., Penkov, S., Cruciani, G., Fedorova, M., & Goracci, L. (2025) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-025-06136-z · Cited by 4
“Many complex lipids are integral components of biological membranes and interact with matrix constituents such as proteins [10] and glycans [11, 12] via non-covalent interactions, including hydrophobic forces, van der Waals interactions, hydrogen bonding, and ionic interactions.”
Conformational Flexibility of Transmembrane Helices: How it Works and Where it Matters
Langosch, D. (2026) · Chemical Reviews · doi:10.1021/acs.chemrev.5c00581 · Cited by 3
Ten questions on membrane biophysics
Pabst, G., Vargas, C., & Keller, S. (2026) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2026.184531 · Cited by 4
Phospholipid membrane interfaces and metal cations, Ca2+ and Cu2+, modulate insulin amyloid fibrillation
Tsurumoto, S., Goto, S., Kasai, T., et al. (2026) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2026.115941 · Cited by 3

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)
DOI: 10.1016/s0005-2736(03)00056-7
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: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 3766 d)
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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Lipid–protein interactions in biological membranes: a structural perspective

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