Contribution of Phosphate Groups to the Dipole Potential of Dimyristoylphosphatidylcholine Membranes

Díaz, Sergio; Lairion, Fabiana; Arroyo, Jesús; Lopez, A.; Disalvo, E.A.

doi:10.1021/la000683w

Cited by 32 publications

(41 citation statements)

References 16 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This result correlates well with the experimental observations presented in Fig. 1b. The influence of the orientation of water molecules forming H bonds on the dipole potential magnitude was mentioned by many authors, who generally pre ferred the molecules positioned close to carboxyl [2,20,21] or phosphate [22] groups of phospholipids. In our previous work we showed that the contribution of phosphate groups to dipole potential agrees well to experimental data, in contrast to carboxyl or carbonyl ones [9].…”

Section: Resultsmentioning

confidence: 99%

Structural factors of lysine and polylysine interaction with lipid membranes

Marukovich

Nesterenko

Ermakov

2015

Biochem. Moscow Suppl. Ser. A

View full text Add to dashboard Cite

Electrostatic effects in lysine and polylysine adsorption at lipid membrane surface were studied. Electrokinetic measurements demonstrated that lysine induces similar dose dependent changes of zeta potential in suspensions of liposomes made from cardiolipin (CL) and phosphatidylserine (PS). These changes correlate well with numerical description of diffuse part of electric double layer by Gouy-Chap man-Stern model in assumption that both potassium cation and lysine molecules determine the ionic strength of the media. Good agreement with the electrokinetic data was found with the isotherm constructed for lysine distribution between bilayer and water with low constant (K d = 1.2 × 10 -3 M -1 ) independently of potassium adsorption (K = 1 M -1 ) on lipid molecules or for their competitive adsorption with the same con stants. Lysine adsorption induces total boundary potential changes of planar bilayer lipid membranes (BLM) from the same lipids registered by the method of intramembranous field compensation. In contrast to surface potential of liposomes in electrokinetic experiments the total boundary potential of BLM remains unchanged up to concentration of lysine that is about 1.5 orders of magnitude higher. This fact corresponds to changes in opposite directions of surface and dipole components of boundary potential. They compensate each other to some extent when lysine adsorbs at the surface. This explanation was supported by molecular dynamic sim ulation of bilayers from DOPS in the presence of lysine. According to the MD simulations, the compensation effect can be attributed to lysine effect on hydrogen bonds of water molecules with phosphate groups of lipids but not with carboxylic groups. A similar "compensation effect" was expected and observed with membranes from CL and PS. The amplitude of dipole effect was about 40 mV due to the lysine-lipid interactions and corresponded well to the amplitude of the slow phase in the boundary potential changes induced by polylysine adsorption on planar BLM. This phase can be attributed to polypeptide conformational changes and/or lipid bilayer restructuring phenomena.

show abstract

Section: Resultsmentioning

confidence: 99%

Structural factors of lysine and polylysine interaction with lipid membranes

Marukovich

Nesterenko

Ermakov

2015

Biochem. Moscow Suppl. Ser. A

View full text Add to dashboard Cite

show abstract

“…Phloretin and sucrose decrease slightly that difference between the two CO populations. In contrast, arbutin produces a notable decrease [106][107][108][109].…”

Section: Data Of Ftir Inmentioning

confidence: 99%

Structural and functional properties of hydration and confined water in membrane interfaces

Disalvo

Lairion

Martini

et al. 2008

Biochimica et Biophysica Acta (BBA) - Biomembranes

195

View full text Add to dashboard Cite

The scope of the present review focuses on the interfacial properties of cell membranes that may establish a link between the membrane and the cytosolic components. We present evidences that the current view of the membrane as a barrier of permeability that contains an aqueous solution of macromolecules may be replaced by one in which the membrane plays a structural and functional role. Although this idea has been previously suggested, the present is the first systematic work that puts into relevance the relation water-membrane in terms of thermodynamic and structural properties of the interphases that cannot be ignored in the understanding of cell function. To pursue this aim, we introduce a new definition of interphase, in which the water is organized in different levels on the surface with different binding energies. Altogether determines the surface free energy necessary for the structural response to changes in the surrounding media. The physical chemical properties of this region are interpreted in terms of hydration water and confined water, which explain the interaction with proteins and could affect the modulation of enzyme activity. Information provided by several methodologies indicates that the organization of the hydration states is not restricted to the membrane plane albeit to a region extending into the cytoplasm, in which polar head groups play a relevant role. In addition, dynamic properties studied by cyclic voltammetry allow one to deduce the energetics of the conformational changes of the lipid head group in relation to the head-head interactions due to the presence of carbonyls and phosphates at the interphase. These groups are, apparently, surrounded by more than one layer of water molecules: a tightly bound shell, that mostly contributes to the dipole potential, and a second one that may be displaced by proteins and osmotic stress. Hydration water around carbonyl and phosphate groups may change by the presence of polyhydroxylated compounds or by changing the chemical groups esterified to the phosphates, mainly choline, ethanolamine or glycerol. Thus, surface membrane properties, such as the dipole potential and the surface pressure, are modulated by the water at the interphase region by changing the structure of the membrane components. An understanding of the properties of the structural water located at the hydration sites and the functional water confined around the polar head groups modulated by the hydrocarbon chains is helpful to interpret and analyze the consequences of water loss at the membranes of dehydrated cells. In this regard, a correlation between the effects of water activity on cell growth and the lipid composition is discussed in terms of the recovery of the cell volume and their viability. Critical analyses of the properties of water at the interface of lipid membranes merging from these results and others from the literature suggest that the interface links the membrane with the aqueous soluble proteins in a functional unit in which the cell may be considered as a compl...

show abstract

“…Thus, water plays a key role in the structural organization of proteins and small peptides. [10][11][12][13][14][15] The lipid bilayer defects could be ascribed to local changes in the packing of the polar head group, because of the difference in hydration of lipids in the gel and in the liquid crystalline state. [16] In this regard, it is important to bear in mind that the changes of water organization at the lipid interphase could affect activity of some proteins.…”

Section: Introductionmentioning

confidence: 99%

FTIR and Raman analysis ofl-cysteine ethyl ester HCl interaction with dipalmitoylphosphatidylcholine in anhydrous and hydrated states

Arias

Tuttolomondo

Díaz

et al. 2015

J. Raman Spectrosc.

View full text Add to dashboard Cite

Interactions of L-cysteine ethyl ester hydrochloride (CE), a bioactive cysteine derivative, with dipalmitoylphosphatidylcholine (DPPC) were investigated. To gain a deeper insight into analyzing L-cysteine ethyl ester HCl interaction with liposomes of DPPC in anhydrous and hydrated states, we performed experimental studies by infrared (Fourier transform infrared spectroscopy) and Raman spectroscopies. The results revealed that the interaction of CE with the phospholipid head groups was the same in absence or presence of water. In both states, the wavenumber of the PO 2 À group and C-N bond of the choline group decreased. This behavior can be ascribed to the replacement of hydration water and binding to the phosphate group. In the Raman spectrum results for the anhydrous and gel states, the S-H stretching band of the CE shifted to lower frequencies with a decrease in its force constant. Biologically active lipophilic molecules such as CE should be studied in terms of their interaction with lipid bilayers prior to the development of advanced lipid carrier systems such as liposomes. The results of these studies provide information on membrane integrity and physicochemical properties that are essential for the rational design of lipidic drug delivery systems.

show abstract

Contribution of Phosphate Groups to the Dipole Potential of Dimyristoylphosphatidylcholine Membranes

Cited by 32 publications

References 16 publications

Structural factors of lysine and polylysine interaction with lipid membranes

Structural factors of lysine and polylysine interaction with lipid membranes

Structural and functional properties of hydration and confined water in membrane interfaces

FTIR and Raman analysis ofl-cysteine ethyl ester HCl interaction with dipalmitoylphosphatidylcholine in anhydrous and hydrated states

Contact Info

Product

Resources

About