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Vitiello, G. Mimicking the Mammalian Plasma Membrane. Encyclopedia. Available online: (accessed on 15 April 2024).
Vitiello G. Mimicking the Mammalian Plasma Membrane. Encyclopedia. Available at: Accessed April 15, 2024.
Vitiello, Giuseppe. "Mimicking the Mammalian Plasma Membrane" Encyclopedia, (accessed April 15, 2024).
Vitiello, G. (2021, February 22). Mimicking the Mammalian Plasma Membrane. In Encyclopedia.
Vitiello, Giuseppe. "Mimicking the Mammalian Plasma Membrane." Encyclopedia. Web. 22 February, 2021.
Mimicking the Mammalian Plasma Membrane

Cell membranes are very complex biological systems including a large variety of lipids and proteins. Therefore, they are difficult to extract and directly investigate with biophysical methods.

mammalian plasma membrane biomimetic lipid membranes

1. Introduction

Cell membranes are the most external cellular envelopes, which separate the cells from the surrounding environment and, in the case of eukaryotic cells, compartmentalize them into different internal organelles [1]. Cell membranes exhibit a complex composition including several different species of lipids and proteins. The lipids, in particular, are responsible for providing the membrane structural scaffold. The amphiphilic structure of the majority of the lipids promotes their self-assembling into a bilayer-like structure (Figure 1). The lipid bilayer incorporates transmembrane proteins across the bilayer hydrophobic region and also provides a hydrophilic and charged surface for the transient or permanent anchoring of soluble proteins (i.e., peripheral proteins) or other biomolecules [2]. In addition, specific interactions between membrane proteins and lipids occur within cell membranes, and they are crucial for several biological processes [2][3]. The lipids are also energy and heat sources and can be signaling molecules [4]. Altogether, the synergistic functions of proteins and lipids enable cell membranes to act as selective barriers, and their proper functioning is vital for the cells [5].

Figure 1. (a) Schematic representation of a lipid bilayer with membrane proteins. Transmembrane proteins are located across the lipid bilayer; peripheral proteins are mainly located at the bilayer surface; in some cases, they can include a fatty acid moiety in their structure, which is embedded in the lipid bilayer. The lipid bilayer is composed of two layers of lipids; the lipid headgroups are reported in red, and the lipid acyl chains are reported in yellow. (b) Structure of the three main classes of lipids in the plasma membrane. As an example of glycerophospholipids and sphingolipids, the chemical structures of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine and N-palmitoleoyl-d-erythro-sphingosylphosphorylcholine are reported, respectively. The lipid hydrophilic headgroup is outlined in red, whereas the lipid hydrophobic acyl chains are outlined in yellow.

2. Applications of Biomimetic Lipid Membranes to Investigate Protein-Lipid or Drug-Lipid Interactions

Lipid-protein interactions play a fundamental role in several biological processes that are vital for the cell. Indeed, proteins can selectively recognize a specific lipid or sense the overall physical properties of cell membranes, e.g., membrane curvature, thickness, or segregated lipid domains [6]. In this context, biomimetic lipid membranes, both in solution [7][8] and on surfaces [9][10], emerged as suitable mammalian plasma membrane models to study protein-lipid interactions through biophysical methods. Indeed, the lipid composition of biomimetic lipid membranes can be suitably tuned to reproduce specific features of cell membranes. This enables the characterization of the impact of specific lipids on membrane-protein interactions [11]. Biomimetic lipid membranes are also largely used as lipid platforms to test drug-membrane interactions, which would occur on the surface of the mammalian plasma membrane. Indeed, more than 60% of the currently marketed drugs target components of the plasma membrane [12].

2.1. Protein-Lipid Interactions

Recently, interactions between lipid membranes and intrinsically disordered proteins have been intensively studied. In particular, the interaction between alfa-synuclein (α-syn) and biomimetic lipid membranes is one of the most studied because of its implications in Parkinson’s disease, a severe neurological disorder. α-syn is a small soluble protein in its physiological state, but it can aggregate and form fibrils that accumulate in the neurons, therefore causing neurodegenerative pathologies [13]. Many studies investigated the role of lipids in favoring the α-syn aggregation into fibrils [14][15][16]. Indeed, α-syn binding to biomimetic membranes was probed by using both lipid membranes in solution and on surfaces, which were prepared with negatively charged phospholipids, such as PS [17][18] or PG [19]. As a result, the α-syn binding affinity for biomimetic membranes is directly correlated to the amount of negatively charged phospholipids in the membrane. This was recently demonstrated by in vitro experiments investigating the alfa-syn binding to small unilamellar vesicles, mimicking synaptic vesicles [20]. Monomeric alfa-syn was shown to interact not only with the lipid headgroups, but also to penetrate the hydrophobic region of supported lipid bilayers prepared with equimolar 1,2-dioleyl-phosphatidyl-glycerol (DOPG) and 1,2-dioleyl-phosphatidyl-ethanolamine (DOPE) [21]. In addition, supported lipid bilayers composed of mixed PC and GM1 ganglioside were recently prepared in order to investigate the selective alfa-syn/GM1 interaction, which induced strong structural rearrangement of the biomimetic membranes (Figure 2a). This observation is a strong indication of the potential critical role of lipid rafts in the biological function of α-syn [22]. Similarly to α-syn, other amyloidogenic proteins and peptides, with an intrinsically disordered structure and a propensity to self-aggregate into fibrils, also known as amyloids, can interact with biomimetic lipid membranes and are involved in human neurodegenerative diseases. Although the mechanisms of amyloid growth and toxicity are still not fully understood, the interaction between amyloidogenic proteins and lipid membranes is believed to favor protein aggregation into first early oligomers and, subsequently, mature fibrils with specific biophysical, structural, and toxicity features [23]. In particular, the interaction between the amyloid β-peptide (Aββ-peptide), which is derived from human islet amyloid polypeptide (IAPP), and biomimetic lipid membranes was recently studied in solution (i.e., giant and large unilamellar vesicles) [24]. The characterization of the interaction between the Aβ peptide (residues 1–42) and large unilamellar vesicles composed of DOPC revealed the role of the zwitterionic lipid membrane in increasing the fibril growth [25]. In addition, a recent study on a supported lipid bilayer composed of POPC showed that the IAPP can initially absorb on the membrane surface and subsequently perturb the membrane structure by extracting lipids [26]. The presence of membrane domains enriched in cholesterol and sphingolipids was also reproduced in biomimetic lipid membranes and resulted in having a strong impact on the interaction with the Aβ peptide [27]. In this context, the characterization by X-ray diffraction of supported lipid membranes made of dimyristoylphosphatidylcholine (DMPC), dimyristoylphosphoserine (DMPS), and cholesterol (at 30 mol%) demonstrated the effect of the membrane lipid composition in modulating the interactions with Aββ(1–42) and Aβ(25–35) fragments [28]. Additional recent studies on Aβ-membrane interaction used vesicles and supported lipid bilayers with a complex lipid composition, including raft lipids such as cholesterol and sphingomyelin (SM), but also polyunsaturated fatty acids (PUFA) (better known as omega-3 lipids), and showed the central role of omega-3 lipids in favoring a deeper internalization of the peptide among the lipid acyl chains and, consequently, hindering its pathogenic self-aggregation [28][29]. Another example of the interaction between a soluble protein and lipid membranes is the recently reported study of the adsorption of the lipid interaction domain (LID) of the Na/H exchanger isoform 1 (NHE1), a mammalian membrane protein, on supported lipid bilayers composed of POPC and 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-L-serine (POPS) [30]. In particular, the lipid membrane was shown to have an important role in inducing protein folding at the membrane surface.

Lipid membranes are also used as platforms to investigate the interaction between the mammalian plasma membrane and viral fusion proteins or peptides. Indeed, enveloped viruses are characterized by glycoproteins in their envelopes, which have the function of favoring the fusion between the virus envelope and the mammalian plasma membrane. This membrane fusion event is fundamental for the virus RNA to enter into the host cell [31]. Short fusion peptides derived from viral glycoproteins gp36 of feline immunodeficiency virus (FIV) [32][33] and gp41 of human immunodeficiency virus (HIV) [34] were recently shown to absorb on both lipid vesicles and supported lipid bilayers composed of either POPC or POPC/SM/CHOL mixtures. In particular, the bilayer lipid composition was found to be decisive in favoring the membrane fusion process promoted by these peptides. Lipid vesicles with composition POPC/SM/CHOL were also used to investigate the membrane fusion mechanism induced by the membranotropic fragments of gB and gH glycoproteins of herpes simplex virus (HSV) type I [35][36][37][38]. Altogether, these studies suggested that viral glycoproteins might target raft domains within the mammalian plasma membrane (Figure 2b). In addition, negatively charged phospholipids, such as PS, can also affect the adsorption and the membrane location of fusion peptides, as shown in a recent study involving POPC/POPS vesicles and peptides derived from the C-terminal domain of HIV-1 viral protein R [39]. Glycoproteins of other enveloped viruses such as influenza or SARS-CoV viruses were also shown to have a strong association with raft-like lipid domains [40][41]. Therefore, the plasma membrane lipid composition has a central role in the mechanism and extent of membrane fusion, i.e., the first step of the viral infection [42].

Figure 2. (a) Schematic representation of the interaction between α-synuclein (α-syn) and supported lipid bilayers composed of either pure 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) or a mixture of DPPC and ganglioside GM1. Neutron reflectometry measurements revealed that GM1 affects the location of α-syn with respect to the biomimetic lipid membrane. Adapted and reprinted with permission from [22], Copyright (2019) Elsevier. (b) Schematic representation of the interaction between the gH625 fusion peptide from the envelope of the herpes simplex virus (HSV) and lipid vesicles with lipid composition mimicking the rafts in the mammalian plasma membrane. Electron paramagnetic spectroscopy measurements revealed that the peptide mainly interacts with the lipid headgroups. Adapted and reprinted with permission from [39], Copyright (2015) Royal Society of Chemistry (RSC).

2.2. Drug-Lipid Interactions

The plasma membrane being among the most external cellular components, the characterization of drug-lipid interactions has a central role in the development of new and more efficient drugs of natural or synthetic origins [43]. Among all, the investigation of the interactions between anticancer drugs and lipid membranes is of particular interest because of the peculiar lipidomic profile of cancer cells, which can be potentially used to design selective antitumoral therapies [44]. Lipid monolayers composed of egg yolk phosphatidylcholine lipids with and without cholesterol were used as biomimetic membranes to characterize their interaction with curcumin, a potential anticancer and ant-inflammatory agent [45]. As a result, curcumin molecules had a condensing effect on the lipid monolayer prepared with only phosphatidylcholine lipids, while the opposite effect was observed when cholesterol was also present in the monolayer. Drug-lipid interactions were also reported for chemotherapeutic agents widely used against cancer such as doxorubicin, paclitaxel, cisplatin, gemcitabine, and vinblastine [46]. These drugs target internal components of cancer cells; therefore, understanding the mechanism through which they interact with the plasma membrane lipids and eventually cross the membrane is of great relevance (Figure 3a). In particular, lipid monolayers prepared with either DMPC or mixtures of DMPC and DMPS were used to show doxorubicin’s preferential interaction with negatively charged membranes [47]. Lipid monolayers were also prepared with natural lipid mixtures directly extracted from doxorubicin-sensitive and doxorubicin-resistant cancer cells [48]. This study showed that lipids extracted from doxorubicin-resistant cancer cells exhibit a higher content of sphingomyelin, phosphatidylinositol lipids, and cholesterol compared to doxorubicin-resistant cancer cells. As a consequence of their different lipid composition, the monolayers produced from the resistant cancer cells are more condensed and rigid, and therefore, these cells might reduce the transport of doxorubicin across their plasma membrane.

Anti-inflammatory drugs are another large class of biologically-active compounds. The study of their interaction with the plasma membrane lipids is of great relevance for understanding their mechanism of action. Tomelin, a non-steroidal anti-inflammatory drug for the treatment of rheumatoid arthrosis, was shown to strongly interact with the DPPC lipid headgroup within both biomimetic lipid membranes in solution and on surfaces [49]. The electrostatic interactions between tomelin molecules and the lipid headgroups, which promote tomelin adsorption on the membrane surface, are believed to be the reason for the great drug efficacy, but also for its related side-effects. Evidence of association with the lipid headgroups was also collected for other more common non-steroidal anti-inflammatory drugs (NSAIDs) such as ibuprofen, naproxen, and diclofenac [50]. In particular, in this study, vesicles composed of DMPS were used as biomimetic lipid membranes.

The membrane localization and orientation of ibuprofen, as well as its influence on membrane properties were recently studied by using solid-state NMR spectroscopy and other biophysical assays on large unilamellar vesicles composed of POPC or a POPC/ cholesterol mixture [51]. The experimental results demonstrated that ibuprofen adopted a mean position in the upper chain/glycerol region of the POPC membrane, oriented with its polar carbonyl group towards the aqueous phase. At the same time, the interaction with the membrane was only marginally altered in the presence of cholesterol, in contrast with a previous study indicating that ibuprofen was expelled from the membrane interface in cholesterol-containing DMPC bilayers [52]. Supported lipid bilayers with different composition (i.e., DLPC and POPC, also in mixture with POPG and cholesterol) were chosen to describe the multi-step interactions between lipid membranes and ibuprofen, as a function of its concentration [53]. As a result, both the chemistry of the lipid headgroups and the packing of lipid acyl chains substantially influence the drug-membrane interactions. Unilamellar vesicles composed of DMPC were also used to understand the effect of aspirin, a commonly used NSAID, on the phase behavior of biomimetic membranes [54]. Neutron scattering measurements indicated that aspirin accelerated both lateral and internal motions, with the more pronounced effect observed for the ordered phase of the neat membrane. In particular, aspirin appeared to have a plasticizing effect on the DMPC membrane dynamics, not only on all the measured time scales, but also in both the gel and fluid lipid phase.

The natural polyphenol resveratrol exhibits potential therapeutic activity with cardioprotective, anti-neurodegenerative, antioxidant, and antitumor action. Recently, these therapeutic actions were suggested be related to resveratrol’s interaction with the plasma membrane. In particular, by using biomimetic membranes in solution composed of egg-PC, SM, and cholesterol at different ratios, resveratrol molecules were found to be mainly located in bilayer domains rich in cholesterol and SM; see Figure 3b [55]. In addition, the impact of resveratrol on the phase transition of vesicles composed of DLPC and DSPC was also reported [56]. As a result, resveratrol abolishes the transition of DLPC and acts as a plasticizer for phospholipids with longer fatty acyl chains. The interaction with biomimetic membranes was also investigated for another natural compound, i.e., quercetin, a naturally-occurring flavonoid, which exhibits beneficial health effects [57]. Quercetin showed a strongly pH-dependent tendency to insert into a biomimetic membrane composed of 1,2-diacyl-sn-glycero-3-phosphocholine, which resulted in significant alterations of the membrane’s functioning.

Figure 3. (a) Schematic representation of the interaction between anticancer drugs and the cell membrane. Anticancer drugs must cross the plasma cell membrane to reach their internal cellular targets. Adapted and reprinted with permission from [46], Copyright (2014) Elsevier. (b) Schematic representation of the interaction of a biomimetic lipid membrane rich in cholesterol and sphingomyelin with resveratrol (RVS), a natural compound with cardioprotective, anti-neurodegenerative, antioxidant, and antitumor action. Adapted and reprinted with permission from [55], Copyright (2016) American Chemical Society (ACS).


  1. Lombard, J. Once upon a time the cell membranes: 175 years of cell boundary research. Biol. Direct. 2014, 9, 32.
  2. De la Serna, J.B.; Schutz, G.J.; Eggeling, C.; Cebecauer, M. There is no simple model of the plasma membrane organization. Front. Cell. Dev. Biol. 2016, 4, 106.
  3. Lundbaek, J.A.; Collingwood, S.A.; Ingólfsson, H.I.; Kapoor, R.; Andersen, O.S. Lipid bilayer regulation of membrane protein function: Gramicidin channels as molecular force probes. J. R. Soc. Interface 2010, 7, 373–395.
  4. Fernandis, A.Z.; Wenk, M.R. Membrane lipids as signaling molecules. Curr. Opin. Lipidol. 2007, 18, 121–129.
  5. Yang, N.J.; Hinner, M.J. Getting across the cell membrane: An overview for small molecules, peptides, and proteins. Methods Mol. Biol. 2015, 1266, 29–53.
  6. Saliba, A.E.; Vonkova, I.; Gavin, A.C. The systematic analysis of protein–lipid interactions comes of age. Nat. Rev. Mol. Cell Biol. 2015, 16, 753–761.
  7. Zahidul, I.M.; Jahangir, A.; Tamba, Y.; Karal, M.A.S.; Yamazaki, M. The single GUV method for revealing the functions of antimicrobial, pore-forming toxin, and cell-penetrating peptides or proteins. Phys. Chem. Chem. Phys. 2014, 30, 15752–15767.
  8. Cheng, B.; Li, Y.; Ma, L.; Wang, Z.; Petersen, R.B.; Zheng, L.; Chen, Y.; Huang, K. Interaction between amyloidogenic proteins and biomembranes in protein misfolding diseases: Mechanisms, contributors, and therapy. Biochem. Biophys. Acta 2018, 1860, 1876–1888.
  9. Luchini, A.; Arleth, L. Protocol for Investigating the Interactions Between Intrinsically Disordered Proteins and Membranes by Neutron Reflectometry. Methods Mol. Biol. 2020, 2141, 569–584.
  10. Elderdfi, M.; Sikorski, A.F. Langmuir-monolayer methodologies for characterizing protein-lipid interactions. Chem. Phys. Lip. 2018, 212, 61–72.
  11. Seddon, A.M.; Curnow, P.; Booth, P.J. Membrane proteins, lipids and detergents: Not just a soap opera. Biochim. Biophys. Acta 2004, 1666, 105–117.
  12. Overington, J.; Al-Lazikani, B.; Hopkins, A. How many drug targets are there? Nat. Rev. Drug Discov. 2006, 5, 993–996.
  13. Meade, R.M.; Fairlie, D.P.; Mason, J.M. Alpha-synuclein structure and Parkinson’s disease—Lessons and emerging principles. Mol. Neurodegener. 2019, 14, 29.
  14. Gilmozzi, V.; Gentile, G.; Castelo Rueda, M.P.; Hicks, A.A.; Pramstaller, P.P.; Zanon, A.; Lévesque, M.; Pichler, I. Interaction of Alpha-Synuclein With Lipids: Mitochondrial Cardiolipin as a Critical Player in the Pathogenesis of Parkinson’s Disease. Front. Neurosci. 2020, 14, 578993.
  15. Hannestad, J.K.; Rocha, S.; Agnarsson, B.; Zhdanov, Z.P.; Wittung-Stafshede, P.; Höök, F. Single-vesicle imaging reveals lipid-selective and stepwise membrane disruption by monomeric α-synuclein. Proc. Natl. Acad. Sci. USA 2020, 117, 14178–14186.
  16. Wildburger, N.C.; Hartke, A.; Schidlitzki, A.; Richter, F. Current Evidence for a Bidirectional Loop Between the Lysosome and Alpha-Synuclein Proteoforms. Front. Cell Dev. Biol. 2020, 8, 1372.
  17. Galvagnion, C.; Buell, A.K.; Meisl, G.; Michaels, T.C.T.; Vendruscolo, M.; Knowles, T.P.J.; Dobson, C.M. Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation. Nat. Chem. Biol. 2015, 11, 229–234.
  18. Hellstrand, E.; Grey, M.; Ainalem, M.L.; Ankner, J.; Forsyth, V.T.; Fragneto, G.; Haertlein, M.; Dauvergne, M.T.; Nilsson, H.; Brundin, P.; et al. Adsorption of α-synuclein to supported lipid bilayers: Positioning and role of electrostatics. ACS Chem. Neurosci. 2013, 16, 1339–1351.
  19. Cholak, E.; Bugge, K.; Khondker, A.; Gauger, K.; Pedraz-Cuesta, E.; Pedersen, M.E.; Bucciarelli, S.; Vestergaard, B.; Pedersen, S.F.; Rheinstädter, M.C.; et al. Avidity within the N-terminal anchor drives α-synuclein membrane interaction and insertion. FASEB J. 2020, 34, 7462–7482.
  20. Das, T.; Eliezer, D. Membrane interactions of intrinsically disordered proteins: The example of alpha-synuclein. Biochem. Biophys. Acta 2019, 1867, 879–889.
  21. Tosatto, L.; Andrighetti, A.O.; Plotegher, N.; Antonini, V.; Tessari, I.; Ricci, L.; Bubacco, L.; Dalla Serra, M. Alpha-synuclein pore forming activity upon membrane association. Biochem. Biophys. Acta 2012, 1818, 2876–2883.
  22. Perissinotto, F.; Rondelli, V.; Parisse, P.; Tormena, N.; Zunino, A.; Almásy, L.; Merkel, D.G.; Bottyán, L.; Sajti, S.; Casalis, L. GM1 Ganglioside role in the interaction of Alpha-synuclein with lipid membranes: Morphology and structure. Biophys. Chem. 2019, 255, 106272.
  23. Bucciantini, M.; Rigacci, S.; Stefani, M. Amyloid Aggregation: Role of Biological Membranes and the Aggregate–Membrane System. J. Phys. Chem. Lett. 2014, 5, 517–527.
  24. Lindberg, D.J.; Wesén, E.; Björkeroth, J.; Rocha, S.; Esbjörner, E.K. Lipid membranes catalyse the fibril formation of the amyloid-β (1–42) peptide through lipid-fibril interactions that reinforce secondary pathways. Biochem. Biophys. Acta 2017, 1859, 1921–1929.
  25. Martel, A.; Antony, L.; Gerelli, Y.; Porcar, L.; Fluitt, A.; Hoffmann, K.; Kiesel, I.; Vivaudou, M.; Fragneto, G.; de Pablo, J.J. Membrane Permeation versus Amyloidogenicity: A Multitechnique Study of Islet Amyloid Polypeptide Interaction with Model Membranes. J. Am. Chem. Soc. 2017, 139, 137–148.
  26. Staneva, G.; Watanabe, C.; Puff, N.; Yordanova, V.; Seigneuret, M.; Angelova, M.I. Amyloid-β Interactions with Lipid Rafts in Biomimetic Systems: A Review of Laboratory Methods. Methods Mol. Biol. 2021, 2187, 47–86.
  27. Dies, H.; Toppozini, L.; Rheinstädter, M.C. Amyloid-β The Interaction between Amyloid-β Peptides and Anionic Lipid Membranes Containing Cholesterol and Melatonin. PLoS ONE 2014, 9, e99124.
  28. Vitiello, G.; Di Marino, S.; D’Ursi, A.M.; D’Errico, G. Omega-3 Fatty Acids Regulate the Interaction of the Alzheimer’s Aβ(25–35) Peptide with Lipid Membranes. Langmuir 2013, 9, 14239–14245.
  29. Emendato, A.; Spadaccini, R.; De Santis, A.; Guerrini, R.; D’Errico, G.; Picone, D. Preferential interaction of the Alzheimer peptide Aβ-(1-42) with Omega-3-containing lipid bilayers: Structure and interaction studies. FEBS Lett. 2016, 590, 582–591.
  30. Hendus-Altenburger, R.; Vogensen, J.; Pedersen, E.S.; Luchini, A.; Araya-Secchi, R.; Bendsoe, A.H.; Prasad, N.S.; Prestel, A.; Cardenas, M.; Pedraz-Cuesta, E.; et al. The intracellular lipid-binding domain of human Na+/H+ exchanger 1 forms a lipid-protein co-structure essential for activity. Commun. Biol. 2020, 3, 731.
  31. Weissenhorn, W.; Hinz, A.; Gaudin, Y. Virus membrane fusion. FEBS Lett. 2007, 581, 2150–2155.
  32. Merlino, A.; Vitiello, G.; Grimaldi, M.; Sica, F.; Busi, E.; Basosi, R.; D’Ursi, A.M.; Fragneto, G.; Paduano, L.; D’Errico, G. Destabilization of lipid membranes by a peptide derived from glycoprotein gp36 of feline immunodeficiency virus: A combined molecular dynamics/experimental study. J. Phys. Chem. B 2012, 116, 401–412.
  33. Vitiello, G.; Fragneto, G.; Petruk, A.A.; Falanga, A.; Galdiero, S.; D’Ursi, A.M.; Merlino, A.; D’Errico, G. Cholesterol modulates the fusogenic activity of a membranotropic domain of the FIV glycoprotein gp36. Soft Matter 2013, 9, 6442–6456.
  34. Oliva, R.; Emendato, A.; Vitiello, G.; De Santis, A.; Grimaldi, M.; D’Ursi, A.M.; Busi, E.; Del Vecchio, P.; Petraccone, L.; D’Errico, G. On the microscopic and mesoscopic perturbations of lipid bilayers upon interaction with the MPER domain of the HIV glycoprotein gp41. Biochem. Biophys. Acta 2016, 1858, 1904–1913.
  35. Galdiero, S.; Falanga, A.; Vitiello, G.; Vitiello, M.; Pedone, C.; D’Errico, G.; Galdiero, M. Role of membranotropic sequences from herpes simplex virus type I glycoproteins B and H in the fusion process. Biochem. Biophys. Acta 2010, 1798, 579–591.
  36. Vitiello, G.; Falanga, A.; Galdiero, M.; Marsh, D.; Galdiero, S.; D’Errico, G. Lipid composition modulates the interaction of peptides deriving from herpes simplex virus type I glycoproteins B and H with biomembranes. Biochem. Biophys. Acta 2011, 1808, 2517–2526.
  37. Falanga, A.; Tarallo, R.; Vitiello, G.; Vitiello, M.; Perillo, E.; Cantisani, M.; D’Errico, G.; Galdiero, M.; Galdiero, S. Biophysical characterization and membrane interaction of the two fusion loops of glycoprotein B from herpes simplex type I virus. PLoS ONE 2012, 7, e32186.
  38. Vitiello, G.; Falanga, A.; Petruk, A.A.; Merlino, A.; Fragneto, G.; Paduano, L.; Galdiero, S.; D’Errico, G. Fusion of raft-like lipid bilayers operated by a membranotropic domain of the HSV-type I glycoprotein gH occurs through a cholesterol-dependent mechanism. Soft Matter 2015, 11, 3003–3016.
  39. Marquette, A.; Leborgne, C.; Schartner, V.; Salnikov, E.; Bechinger, B.; Kichler, A. Peptides derived from the C-terminal domain of HIV-1 Viral Protein R in lipid bilayers: Structure, membrane positioning and gene delivery. Biochem. Biophys. Acta 2020, 1862, 183149.
  40. Levental, I.; Grzybek, M.; Simons, K. Raft domains of variable properties and compositions in plasma membrane vesicles. Proc. Natl. Acad. Sci. USA 2011, 108, 11411–11416.
  41. Vieira, F.S.; Corrêa, G.; Einicker-Lamas, M.; Coutinho-Silva, R. Host-cell lipid rafts: A safe door for micro-organisms? Biol. Cell 2010, 102, 391–407.
  42. Meher, G.; Chakraborty, H. Membrane Composition Modulates Fusion by Altering Membrane Properties and Fusion Peptide Structure. J. Membr. Biol. 2019, 252, 261–272.
  43. Seddon, A.M.; Casey, D.; Law, R.V.; Gee, A.; Templer, R.H.; Ces, O. Drug interactions with lipid membranes. Chem. Soc. Rev. 2009, 38, 2509–2519.
  44. Alves, A.C.; Ribeiro, D.; Nunes, C.; Reis, S. Biophysics in cancer: The relevance of drug-membrane interaction studies. Biochem. Biophys. Acta 2016, 1858, 2231–2244.
  45. Karewicz, A.; Bielska, D.; Gzyl-Malcher, B.; Kepczynski, M.; Lach, R.; Nowakowska, M. Interaction of curcumin with lipid monolayers and liposomal bilayers. Coll. Surf. B 2011, 88, 231–239.
  46. Bourgaux, C.; Couvreur, P. Interactions of anticancer drugs with biomembranes: What can we learn from model membranes? J. Control. Release 2014, 190, 127–138.
  47. Matyszewska, D.; Nazaruk, E.; Campbell, R.A. Interactions of anticancer drugs doxorubicin and idarubicin with lipid monolayers: New insight into the composition, structure and morphology. J. Colloid Interface Sci. 2021, 581, 403–416.
  48. Peetla, C.; Bhave, R.; Vijayaraghavalu, S.; Stine, A.; Kooijman, E.; Labhasetwar, V. Drug Resistance in Breast Cancer Cells: Biophysical Characterization of and Doxorubicin Interactions with Membrane Lipids. Mol. Pharm. 2010, 7, 2334–2348.
  49. Nunes, C.; Brezesinski, G.; Lopes, D.; Lima, J.L.F.C.; Reis, S.; Lúcio, M. Lipid–Drug Interaction: Biophysical Effects of Tolmetin on Membrane Mimetic Systems of Different Dimensionality. J. Phys. Chem. B 2011, 115, 12615–12623.
  50. Manrique-Moreno, M.; Heinbockel, L.; Suwalsky, M.; Garidel, P.; Brandenburg, K. Biophysical study of the non-steroidal anti-inflammatory drugs (NSAID) ibuprofen, naproxen and diclofenac with phosphatidylserine bilayer membranes. Biochem. Biophys. Acta 2016, 1858, 2123–2131.
  51. Kremkow, J.; Luck, M.; Huster, D.; Müller, P.; Scheidt, H.A. Membrane Interaction of Ibuprofen with Cholesterol-Containing Lipid Membranes. Biomolecules 2020, 10, 1384.
  52. Khajeh, A.; Modarress, H. The influence of cholesterol on interactions and dynamics of ibuprofen in a lipid bilayer. Biochem. Biophys. Acta 2014, 1838, 2431–2438.
  53. Sun, S.; Sendecki, A.M.; Pullanchery, S.; Huang, D.; Yang, T.; Cremer, P.S. Multistep Interactions between Ibuprofen and Lipid Membranes. Langmuir 2018, 34, 10782–10792.
  54. Sharma, V.K.; Mamontov, E.; Ohl, M.; Tyagi, M. Incorporation of aspirin modulates the dynamical and phase behavior of the phospholipid membrane. Phys. Chem. Chem. Phys. 2017, 19, 2514–2524.
  55. Neves, A.R.; Nunes, C.; Amenitsch, H.; Reis, S. Resveratrol Interaction with Lipid Bilayers: A Synchrotron X-ray Scattering Study. Langmuir 2016, 32, 12914–12922.
  56. Nur, S.; Nur, F.; Alsamarah, A.; Chatterjee, P.; Nur, N.; Moreno, J.; Luo, L.; Lambros, M. Interaction of Resveratrol with Lipid Membranes. Biophys. J. 2016, 110, 411a.
  57. Kruszewski, M.; Kusaczuk, M.; Kotyńska, J.; Gál, M.; Krętowski, R.; Cechowska-Pasko, M.; Naumowicz, M. The effect of quercetin on the electrical properties of model lipid membranes and human glioblastoma cells. Bioelectrochemistry 2018, 124, 133–141.
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