Intermolecular interactions in lipid/carotenoid monolayers.
Ontology highlight
ABSTRACT:
SUBMITTER: Tomoaia-Cotisel M
PROVIDER: S-EPMC1148631 | biostudies-other | 1987 Dec
REPOSITORIES: biostudies-other
Similar Datasets
Project description:Menaquinones (MK) are hydrophobic molecules that consist of a naphthoquinone headgroup and a repeating isoprenyl side chain and are cofactors used in bacterial electron transport systems to generate cellular energy. We have previously demonstrated that the folded conformation of truncated MK homologues, MK-1 and MK-2, in both solution and reverse micelle microemulsions depended on environment. There is little information on how MKs associate with phospholipids in a model membrane system and how MKs affect phospholipid organization. In this manuscript, we used a combination of Langmuir monolayer studies and molecular dynamics (MD) simulations to probe these questions on truncated MK homologues, MK-1 through MK-4 within a model membrane. We observed that truncated MKs reside farther away from the interfacial water than ubiquinones are are located closer to the phospholipid tails. We also observed that phospholipid packing does not change at physiological pressure in the presence of truncated MKs, though a difference in phospholipid packing has been observed in the presence of ubiquinones. We found through MD simulations that for truncated MKs, the folded conformation varied, but MKs location and association with the bilayer remained unchanged at physiological conditions regardless of side chain length. Combined, this manuscript provides fundamental information, both experimental and computational, on the location, association, and conformation of truncated MK homologues in model membrane environments relevant to bacterial energy production.
| S-EPMC8470443 | biostudies-literature
Project description:Quantitative analysis of the influence of intermolecular interactions on the response of electroactive binary monolayers, incorporating the presence of electroinactive coadsorbed species and Marcus-Hush kinetic formalism, has been deduced as an extension of previous models. An expression for the current-potential relationship in terms of two global phenomenological interaction parameters and the apparent charge-transfer rate constant and formal potential has been obtained and applied to multipotential chronoamperometry for the analysis of intermolecular interaction effects on the kinetics of the charge transfer. Experimental verification of the theoretical framework has been performed with binary ferrocenylundecanethiol/decanethiol monolayers on gold and platinum substrates for different coverage degrees of the redox probe. The increase of the ferrocene coverage gives rise to a slowing down of the charge-transfer process through a decrease of the apparent rate constant above a 90% for gold and platinum electrodes when the surface coverage increases from 1-2 to 15-30%. Significant differences in the magnitude of intermolecular interactions and the symmetry degree of the charge-transfer process are observed between gold and platinum electrodes. Moreover, for high surface coverages of ferrocene, two different domains appear, from which it is possible to carry out a kinetic discrimination of the two responses. Values of the interaction and kinetic parameters have been obtained for the different monolayers under study, and the limit of applicability of this treatment is discussed.
| S-EPMC6641222 | biostudies-literature
Project description:This work investigates the discrimination of lipid monolayers by the ovine antimicrobial peptide SMAP-29 and compares it to that of the human LL-37 peptide. Fluid phospholipid monolayers were formed in a Langmuir trough and subsequently studied with the X-ray scattering techniques of X-ray reflectivity and grazing incidence X-ray diffraction. Any changes in the phospholipid structure after injection of peptide under the monolayer were considered to be due to interactions between the peptides and lipids. The data show that SMAP-29 discriminates against negatively charged phospholipids in a similar way to LL-37. However, it is even more interesting to note that despite a higher concentration of SMAP-29 near the monolayer, ensured by its greater charge as compared to LL-37, the amount of SMAP-29 needed to observe monolayer disruption was around three and a half times the number of molecules of LL-37 used to see similar changes with the same system. This result suggests that the structure, amino acid sequence or size of the peptide may well be as important as electrical charge and therefore gives many implications for the further study of antimicrobial peptides with regards to novel drug design and development.
| S-EPMC2838942 | biostudies-literature
Project description:The size distribution of domains in phase-separated lung surfactant monolayers influences monolayer viscoelasticity and compressibility which, in turn, influence monolayer collapse and set the compression at which the minimum surface tension is reached. The surfactant-specific protein SP-B decreases the mean domain size and polydispersity as shown by fluorescence microscopy. From the images, the line tension and dipole density difference are determined by comparing the measured size distributions with a theory derived by minimizing the free energy associated with the domain energy and mixing entropy. We find that SP-B increases the line tension, dipole density difference, and the compressibility modulus at surface pressures up to the squeeze-out pressure. The increase in line tension due to SP-B indicates the protein avoids domain boundaries due to its solubility in the more fluid regions of the film.
| S-EPMC3250676 | biostudies-literature
Project description:Members of the Hsp90 and Hsp70 families of molecular chaperones are imp\ortant for the maintenance of protein homeostasis and cellular recovery following environmental stresses, such as heat and oxidative stress. Moreover, the two chaperones can collaborate in protein remodeling and activation. In higher eukaryotes, Hsp90 and Hsp70 form a functionally active complex with Hop (Hsp90-Hsp70 organizing protein) acting as a bridge between the two chaperones. In bacteria, which do not contain a Hop homolog, Hsp90 and Hsp70, DnaK, directly interact during protein remodeling. Although yeast possesses a Hop-like protein, Sti1, Hsp90, and Hsp70 can directly interact in yeast in the absence of Sti1. Previous studies showed that residues in the middle domain of Escherichia coli Hsp90 are important for interaction with the J-protein binding region of DnaK. The results did not distinguish between the possibility that (i) these sites were involved in direct interaction and (ii) the residues in these sites participate in conformational changes which are transduced to other sites on Hsp90 and DnaK that are involved in the direct interaction. Here we show by crosslinking experiments that the direct interaction is between a site in the middle domain of Hsp90 and the J-protein binding site of Hsp70 in both E. coli and yeast. Moreover, J-protein promotes the Hsp70-Hsp90 interaction in the presence of ATP, likely by converting Hsp70 into the ADP-bound conformation. The identification of the protein-protein interaction site is anticipated to lead to a better understanding of the collaboration between the two chaperones in protein remodeling.
| S-EPMC6599576 | biostudies-literature
Project description:Surfactants at air/water interfaces are often subjected to mechanical stresses as the interfaces they occupy are reduced in area. The most well characterized forms of stress relaxation in these systems are first order phase transitions from lower density to higher density phases. Here we study stress relaxation in lipid monolayers that occurs once chemical phase transitions have been exhausted. At these highly compressed states, the monolayer undergoes global mechanical relaxations termed collapse. By studying four different types of monolayers, we determine that collapse modes are most closely linked to in-plane rigidity. We characterize the rigidity of the monolayer by analyzing in-plane morphology on numerous length scales. More rigid monolayers collapse out-of-plane via a hard elastic mode similar to an elastic membrane, while softer monolayers relax in-plane by shearing.
| S-EPMC2720559 | biostudies-literature
Project description:The interactions between ions and lipid monolayers have captivated the attention of biologists and chemists alike for almost a century. In the absence of experimentally accessible concentration profiles, the electrolyte adsorption remains the most informative quantitative characteristic of the ion-lipid interactions. However, there is no established procedure to obtain the electrolyte adsorption on spread lipid monolayers. As a result, in the literature, the ion-lipid monolayer interactions are discussed qualitatively, based on the electrolyte effect on more easily accessible variables, e.g., surface tension. In this letter, we demonstrate how the electrolyte adsorption on lipid monolayers can be obtained experimentally. The procedure requires combining surface pressure versus molecular area compression isotherms with spreading pressure data. For the first time, we report an adsorption isotherm of NaCl on a lipid monolayer as a function of the density of the monolayer. The leading interactions seem to be the osmotic effect from the lipid head groups in the surface layer and ion-lipid association.
| S-EPMC10226113 | biostudies-literature
Project description:Collapse of homogeneous lipid monolayers is known to proceed via wrinkling/buckling, followed by folding into bilayers in water. For heterogeneous monolayers with phase coexistence, the mechanism of collapse remains unclear. Here, we investigated collapse of lipid monolayers with coexisting liquid-liquid and liquid-solid domains using molecular dynamics simulations. The MARTINI coarse-grained model was employed to simulate monolayers of ∼80 nm in lateral dimension for 10-25 μs. The monolayer minimum surface tension decreased in the presence of solid domains, especially if they percolated. Liquid-ordered domains facilitated monolayer collapse due to the spontaneous curvature induced at a high cholesterol concentration. Upon collapse, bilayer folds formed in the liquid (disordered) phase; curved domains shifted the nucleation sites toward the phase boundary. The liquid (disordered) phase was preferentially transferred into bilayers, in agreement with the squeeze-out hypothesis. As a result, the composition and phase distribution were altered in the monolayer in equilibrium with bilayers compared to a flat monolayer at the same surface tension. The composition and phase behavior of the bilayers depended on the degree of monolayer compression. The monolayer-bilayer connection region was enriched in unsaturated lipids. Percolation of solid domains slowed down monolayer collapse by several orders of magnitude. These results are important for understanding the mechanism of two-to-three-dimensional transformations in heterogeneous thin films and the role of lateral organization in biological membranes. The study is directly relevant for the function of lung surfactant, and can explain the role of nanodomains in its surface activity and inhibition by an increased cholesterol concentration.
| S-EPMC4156665 | biostudies-literature
Project description:The lining of the alveoli is covered by pulmonary surfactant, a complex mixture of surface-active lipids and proteins that enables efficient gas exchange between inhaled air and the circulation. Despite decades of advancements in the study of the pulmonary surfactant, the molecular scale behavior of the surfactant and the inherent role of the number of different lipids and proteins in surfactant behavior are not fully understood. The most important proteins in this complex system are the surfactant proteins SP-B and SP-C. Given this, in this work we performed nonequilibrium all-atom molecular dynamics simulations to study the interplay of SP-B and SP-C with multicomponent lipid monolayers mimicking the pulmonary surfactant in composition. The simulations were complemented by z-scan fluorescence correlation spectroscopy and atomic force microscopy measurements. Our state-of-the-art simulation model reproduces experimental pressure-area isotherms and lateral diffusion coefficients. In agreement with previous research, the inclusion of either SP-B and SP-C increases surface pressure, and our simulations provide a molecular scale explanation for this effect: The proteins display preferential lipid interactions with phosphatidylglycerol, they reside predominantly in the lipid acyl chain region, and they partition into the liquid expanded phase or even induce it in an otherwise packed monolayer. The latter effect is also visible in our atomic force microscopy images. The research done contributes to a better understanding of the roles of specific lipids and proteins in surfactant function, thus helping to develop better synthetic products for surfactant replacement therapy used in the treatment of many fatal lung-related injuries and diseases.
| S-EPMC10061932 | biostudies-literature
Project description:Mixing the liquids hexafluorobenzene (1) and 1,3,5-trimethylbenzene (mesitylene, 2) results in a crystalline solid with a melting point of 34 °C. The solid consists of alternating π-π stacked pillars of both aromatics. This simple experiment can be used to visually demonstrate the existence and the effect of noncovalent intermolecular π-π stacking interactions. Both benzene derivatives are relatively benign and widely available, and the experiment can be performed within minutes for less than $15 when done on a 22 mL scale (total volume). The demonstration is very robust, as 1:2 mixtures in volume ratios between 2/3 and 3/2 all give a visually similar result (molar ratios of 1.8-0.8). Substituting 2 with the liquid aromatics o-xylene, p-xylene, and aniline also resulted in the formation of a crystalline solid, while using many other liquid aromatics did not.
| S-EPMC7876799 | biostudies-literature