Regulation of Antimicrobial Peptide Activity via Tuning Deformation Fields by Membrane-Deforming Inclusions

Kondrashov, Oleg V.; Akimov, Sergey A.

doi:10.3390/ijms23010326

Cited by 9 publications

(19 citation statements)

References 65 publications

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“…Thus, it seems that, in biological membranes, relatively long-range membranemediated interactions should involve multiple proteins. However, as we showed recently [70], the typical energy of membrane-mediated interactions involving peripheral membrane inclusions is about an order of magnitude smaller than the energy of interactions of transmembrane inclusions. If transmembrane and peripheral proteins have similar surface concentrations, the contribution of peripheral proteins to the total energy of membrane-mediated interactions should be small.…”

Section: Discussionmentioning

confidence: 53%

Hydrophobic Mismatch Controls the Mode of Membrane-Mediated Interactions of Transmembrane Peptides

2022

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Various cellular processes require the concerted cooperative action of proteins. The possibility for such synchronization implies the occurrence of specific long-range interactions between the involved protein participants. Bilayer lipid membranes can mediate protein–protein interactions via relatively long-range elastic deformations induced by the incorporated proteins. We considered the interactions between transmembrane peptides mediated by elastic deformations using the framework of the theory of elasticity of lipid membranes. An effective peptide shape was assumed to be cylindrical, hourglass-like, or barrel-like. The interaction potentials were obtained for membranes of different thicknesses and elastic rigidities. Cylindrically shaped peptides manifest almost neutral average interactions—they attract each other at short distances and repel at large ones, independently of membrane thickness or rigidity. The hourglass-like peptides repel each other in thin bilayers and strongly attract each other in thicker bilayers. On the contrary, the barrel-like peptides repel each other in thick bilayers and attract each other in thinner membranes. These results potentially provide possible mechanisms of control for the mode of protein–protein interactions in membrane domains with different bilayer thicknesses.

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Section: Discussionmentioning

confidence: 53%

Hydrophobic Mismatch Controls the Mode of Membrane-Mediated Interactions of Transmembrane Peptides

2022

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“…deform the membrane [20,21]. The lateral length of deformation decay in "conventional" membranes (e.g., formed from dioleoylphosphatidylcholine, DOPC) is of the order of several nanometers [21][22][23]. When the membrane-deforming objects are far-separated, their induced deformations are independent, and their energy is additive.…”

Section: Introductionmentioning

confidence: 99%

“…When the membrane-deforming objects are far-separated, their induced deformations are independent, and their energy is additive. Upon approaching, the deformed zones near the inclusions overlap; the overlapping leads to an effective membrane-mediated lateral interaction [22,23] on the distances of several nanometers, that exceeds typical distances of interactions like screened Debye, van der Waals and dipole-dipole interactions under physiological conditions [24][25][26][27]. The membrane-mediated interaction is significant at large surface concentrations of inclusions.…”

Section: Introductionmentioning

confidence: 99%

“…Spatial distribution of membrane deformations induced by inclusions can be determined in a framework of an adequate theory of elasticity. Such theories formulate possible deformational modes of the considered elastic medium (lipid membrane), and relate deformations and surface density of the elastic energy [20][21][22][23]. The total elastic energy thus becomes a functional on the surface density of the elastic energy.…”

Section: Introductionmentioning

confidence: 99%

“…Such rigid membrane inclusions are supposed to impose boundary conditions onto the deformations. In this elastic approach, details of the structure and configuration of the membrane-embedded peptide or protein are completely reflected by the boundary conditions they impose onto the membrane deformations [20][21][22][23], for example, an orientation of lipid molecules and local membrane thickness. Utilizing experimental data on the dependence of membrane thickness on the surface concentration of inclusions, our developed model principally allows the obtaining of boundary conditions imposed by amphipathic peptides and transmembrane peptides.…”

Section: Introductionmentioning

confidence: 99%

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Alteration of Average Thickness of Lipid Bilayer by Membrane-Deforming Inclusions

Kondrashov,

Akimov

2023

Biomolecules

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Thickness of lipid bilayer membranes is a key physical parameter determining membrane permeability and stability with respect to formation of through pores. Most membrane inclusions or impurities like amphipathic peptides, transmembrane peptides, lipid inclusions of a different molecular shape, lipid domains, and protein-lipid domains, locally deform the membrane. The detailed structure of the locally deformed region of the membrane is a kind of “fingerprint” for the inclusion type. However, most experimental methods allow determining only averaged parameters of membranes with incorporated inclusions, thus preventing the direct obtaining of the characteristics of the inclusion. Here we developed a model that allows the obtaining of characteristic parameters of three types of membrane inclusions (amphipathic peptides, transmembrane peptides, monolayer lipid patches) from experimentally observable dependencies of the average thickness of lipid bilayer on the surface concentration of the inclusions. In the case of amphipathic peptides, the model provided the peptide parameters that were in qualitative agreement with the available experimental data.

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Effect of solid support and membrane tension on adsorption and lateral interaction of amphipathic peptides

Kondrashov

Akimov

2022

The Journal of Chemical Physics

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A wide class of antimicrobial amphipathic peptides is aimed to selectively form through pores in bacterial membranes. The partial incorporation of the peptides into the lipid monolayer leads to elastic deformation of the membrane. The deformation influences both the adsorption of the peptides and their lateral interaction. Detailed study of pore formation mechanisms requires an accurate determination of the surface concentration of the peptides at their given bulk concentration. Widely used methods to register the adsorption are atomic force microscopy (AFM), surface plasmon resonance refractometry (SPRR), and inner field compensation (IFC). AFM and SPRR utilize membranes deposited onto a solid support, while IFC operates with model membranes under substantial lateral tension. Here, we theoretically studied the effect of the solid support and lateral tension on the elastic deformations of the membrane induced by partially incorporated amphipathic peptides, and thus on the peptide adsorption energy and lateral interaction. We demonstrated that under conditions typical for AFM, SPRR, and IFC the adsorption energy can increase by up to 1.5 kBT per peptide leading to about 4 times decreased surface concentration as compared to free-standing tensionless membranes. In addition, the effective lateral size of the peptide molecule increases by about 10 %, which can have an impact on the quantitative description of the adsorption isotherms. Our results allow estimating the effects of the solid support and lateral tension on the adsorption and interaction of amphipathic peptides at the membrane surface and taking them into account in interpretation of experimental observations.

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Regulation of Antimicrobial Peptide Activity via Tuning Deformation Fields by Membrane-Deforming Inclusions

Cited by 9 publications

References 65 publications

Hydrophobic Mismatch Controls the Mode of Membrane-Mediated Interactions of Transmembrane Peptides

Hydrophobic Mismatch Controls the Mode of Membrane-Mediated Interactions of Transmembrane Peptides

Alteration of Average Thickness of Lipid Bilayer by Membrane-Deforming Inclusions

Effect of solid support and membrane tension on adsorption and lateral interaction of amphipathic peptides

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