Interactions of surfactants with lipid membranes

Heerklotz, Heiko

doi:10.1017/s0033583508004721

Cited by 273 publications

(307 citation statements)

References 294 publications

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“…Many of the so-called integral or transmembrane proteins completely cross the lipidic bilayer and, due to the strong hydrophobic interaction with the phospholipids, can only be removed with the use of detergents-tensoactive compounds which have the ability to decrease the lipid-lipid and lipidprotein interactions during the protein solubilization process (Gennis 1989;Le Maire et al 2000;Santos and Ciancaglini 2000;Santos et al 2002;Magalhães et al 2003;Schuck et al 2003;Heerklotz 2008). On the other hand, peripheral or extrinsic proteins have a superficial interaction with the polar heads of the membrane lipids and can be removed simply by a change in ionic strength or pH.…”

Section: Purification or Expression Of The Membrane Proteinmentioning

confidence: 99%

Proteoliposomes in nanobiotechnology

et al. 2012

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Proteoliposomes are systems that mimic lipid membranes (liposomes) to which a protein has been incorporated or inserted. During the last decade, these systems have gained prominence as tools for biophysical studies on lipid-protein interactions as well as for their biotechnological applications. Proteoliposomes have a major advantage when compared with natural membrane systems, since they can be obtained with a smaller number of lipidic (and protein) components, facilitating the design and interpretation of certain experiments. However, they have the disadvantage of requiring methodological standardization for incorporation of each specific protein, and the need to verify that the reconstitution procedure has yielded the correct orientation of the protein in the proteoliposome system with recovery of its functional activity. In this review, we chose two proteins under study in our laboratory to exemplify the steps necessary for the standardization of the reconstitution of membrane proteins in liposome systems: (1) alkaline phosphatase, a protein with a glycosylphosphatidylinositol anchor, and (2) Na,K-ATPase, an integral membrane protein. In these examples, we focus on the production of the specific proteoliposomes, as well as on their biochemical and biophysical characterization, with emphasis on studies of lipid-protein interactions. We conclude the chapter by highlighting current prospects of this technology for biotechnological applications, including the construction of nanosensors and of a multiprotein nanovesicular biomimetic to study the processes of initiation of skeletal mineralization.

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Section: Purification or Expression Of The Membrane Proteinmentioning

confidence: 99%

Proteoliposomes in nanobiotechnology

et al. 2012

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“…The interaction between phospholipid vesicle membrane and surfactant is of great interest from the standpoints of the solubilization and the reconstitution of membrane proteins, and hence, many researchers have reviewed about it [1][2][3][4][5][6] . In general, the nonionic surfactants have been widely used for this purpose [7][8][9][10][11][12][13][14][15][16][17] .…”

Section: Introductionmentioning

confidence: 99%

Effect of Functional Groups on Incorporation Behavior of Amino Acid-Type Surfactant into Phospholipid Vesicle Membrane

et al. 2009

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The incorporation behaviors of some N-dodecanoyl amino acid-type surfactants into L-adipalmitoylphosphatidylcholine (DPPC) vesicles in aqueous solution were investigated. From the leakage measurements of a vesicle-entrapped fluorescence probe, it was found that these surfactants did not affect the DPPC vesicle so much at a very low concentration less than a one-tenth of the critical micelle concentration (CMC), but caused a significant release of the probe form the vesicles even at just below the CMC. The leakage induced by amino acid-type surfactants was promoted by increasing hydrophobicity of the amino acid. However the polarization of DPH embedded in the DPPC membrane was almost unchanged by incorporation of the surfactants at the concentration below the CMC except for the Ndodecanoylphenylalanine system. The binding enthalpy and the binding constant of the surfactant to DPPC vesicles were estimated by isothermal titration calorimetry. While the binding enthalpy was independent of the kind of surfactant, the binding constant increases with increasing hydrophobicity of the amino acid species in the surfactants. The molar ratio of bound surfactant to DPPC molecule in the saturated state was much greater than that for sodium dodecyl sulfate system. Further the ratio was not influenced by the structure of the amino acid side chain.

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“…The drastic increase of the association constant in step 2 is thought to be due to the smooth insertion of AmB into the membrane via the complex of deoxycholate micelles and the hydrophobic region of the lipid membrane. 41 Also the dissociation constants in step 1 and 2 (kd1, kd2) of the Fungizone to ergosterol-containing membrane increased substantially, indicating that the dissociation rate of Fungizone to the ergosterol-containing membrane would increase with an increase in temperature. In total, however, no obvious change of affinity Table 4 Association (ka1 and ka2), dissociation (kd1 and kd2) rate constants and affinity constant (K) determined by numerical integration using the two-state reaction model (n = 3) at 37 C constant by temperature could be observed for the affinity of Fungizone to the lipid membranes.…”

Section: Binding Characteristic Of Additive and Temperature Dependencmentioning

confidence: 95%