Modeling the interplay between protein and lipid aggregation in supported membranes

Salas, Pablo González de Prado; Encinar, Mario; Alonso, Alvaro; Vélez, Marisela; Tarazona, P.

doi:10.1016/j.chemphyslip.2014.06.006

Cited by 8 publications

(6 citation statements)

References 55 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…How does this dissipated energy affect the membrane? There is experimental evidence that FtsZ filaments attached to a supported lipid bilayer affect the shape of lipid domains and that the segregated lipids also influence the distribution and shape of the filaments ( González de Prado Salas et al, 2015 ). Modeling this behavior requires considering filament torsion, monomer exchange, lateral interactions, and preferential curvature ( Gonzalez de Prado Salas et al, 2014 ), and the tendency of the lipids to segregate into domains ( Figure 2 ).…”

Section: Ftszmentioning

confidence: 99%

How Does the Spatial Confinement of FtsZ to a Membrane Surface Affect Its Polymerization Properties and Function?

Vélez

2022

Front. Microbiol.

Self Cite

View full text Add to dashboard Cite

FtsZ is the cytoskeletal protein that organizes the formation of the septal ring and orchestrates bacterial cell division. Its association to the membrane is essential for its function. In this mini-review I will address the question of how this association can interfere with the structure and dynamic properties of the filaments and argue that its dynamics could also remodel the underlying lipid membrane through its activity. Thus, lipid rearrangement might need to be considered when trying to understand FtsZ’s function. This new element could help understand how FtsZ assembly coordinates positioning and recruitment of the proteins forming the septal ring inside the cell with the activity of the machinery involved in peptidoglycan synthesis located in the periplasmic space.

show abstract

Section: Ftszmentioning

confidence: 99%

How Does the Spatial Confinement of FtsZ to a Membrane Surface Affect Its Polymerization Properties and Function?

Vélez

2022

Front. Microbiol.

Self Cite

View full text Add to dashboard Cite

show abstract

“…41,42 Many other examples can be found. 28,[43][44][45][46] For these reasons, enzymatic conversion of proteins complicated by their aggregation is expected to be studied experimentally in the nearest future. From this perspective, the work presented herein can be classified as forefront research.…”

Section: Resultsmentioning

confidence: 99%

Kinetics of Single-Enzyme Reactions on Vesicles: Role of Substrate Aggregation

Zhdanov

2015

Biophys. Rev. Lett.

View full text Add to dashboard Cite

Enzymatic reactions occurring in vivo on lipid membranes can be influenced by various factors including macromolecular crowding in general and substrate aggregation in particular. In academic studies, the role of these factors can experimentally be clarified by tracking single-enzyme kinetics occurring on individual lipid vesicles. To extend the conceptual basis for such experiments, we analyze herein the corresponding kinetics mathematically with emphasis on the role of substrate aggregation. In general, the aggregation may occur on different length scales. Small aggregates may e.g. contain a few proteins or peptides while large aggregates may be mesoscopic as in the case of lipid domains which can be formed in the membranes composed of different lipids. We present a kinetic model describing comprehensively the effect of aggregation of the former type on the dependence of the reaction rate on substrate membrane concentration. The results obtained with physically reasonable parameters indicate that the aggregationrelated deviations from the conventional Michaelis-Menten kinetics may be appreciable. Special Issue Comments:This theoretical article is focused on single-enzyme reactions occurring in parallel with substrate aggregation on individual vesicles. This subject is related to a few Special Issue articles concerning enzyme dynamics 6,7 and function 8 and mathematical aspects of stochastic kinetics. 9

show abstract

“…The particular choice of the arguments of the intermolecular potential in its new form is in accord with those of the interaction potential between a pair of protein monomers forming a lipid bilayer, in which the pairwise intermolecular potential is a function of the relative position of the two protein particles and the orientation of each of the particles. 47,53 As a consequence of the foregoing discussion, the net free-energy ψ b of the cylindrical body of the micelle can be expressed as

ψ_{b} = true \int_{0}^{L} \frac{1}{2} (\int_{0}^{2 π} ℰ false(s, θ false) normald θ) scriptD false(s false) normald s,

where the integrand of the inner integral,

ℰ

( s , θ ), is

ℰ false(s, θ false) = true \int_{0}^{L} \int_{0}^{2 π} 2 \overset{Ω}{true} false(ℋ_{1}, ℋ_{2}, ℋ_{3}, ℋ_{4} false) D (t) normald η normald t,

with

ℋ_{1} = ε^{- 2} | boldχ false(s false) - boldχ false(t false) |^{2}

ℋ_{2} = boldχ false(s false) - boldχ false(t false) false) \cdot boldd false(s, θ false)

ℋ_{3} = boldχ false(s false) - boldχ false(t false) false) \cdot boldd false(t, η false)

, and

ℋ_{4} = boldd false(s, θ false) \cdot boldd false(t, η false)

. Eq.…”

Section: Micro-mechanical Modelmentioning

confidence: 99%

Micro-mechanical, continuum-mechanical, and AFM-based descriptions of elasticity in open cylindrical micellar filaments

Asgari

2017

Soft Matter

View full text Add to dashboard Cite

We present theoretical and experimental descriptions of the elasticity of cylindrical micellar filaments using micro-mechanical and continuum theories, and Atomic Force Microscopy. Following our micro-mechanical elasticity model for micellar filaments [Asgari, Eur. Phys. J. E 2015, 38(9)], the elastic bending energy of hemispherical end caps is found. The continuum description of the elastic bending energy of a cylindrical micellar filament is also derived using constrained Cosserat rod theory. While the continuum approach provides macroscopic description of the strain energy of the micellar filament, the micro-mechanical approach has a microscopic view of the filament, and provides expressions for kinetic variables based on a selected interaction potential between the molecules comprising the filament. Our model predicts the dependence of the elastic modulus of the micellar filaments on their diameter, which agrees with previous experimental observations. Atomic force microscopy is applied to estimate the elastic modulus of the filaments using force volume analysis. The obtained values of elastic modulus yield the persistence length of micellar filaments on the same order of the previously reported values. Consistent with previous studies, our results indicate that semi-flexible linear micelles have a relatively large local strain energy at their end points, which explains their tendency to fuse to minimize the number of end caps at relatively low total surfactant volume fractions. Also, the elastic modulus of micellar filaments was found to increase when the indentation frequency increases, a finding which agrees with previous rheological observations on the bulk shear modulus of micellar solutions.

show abstract

Modeling the interplay between protein and lipid aggregation in supported membranes

Cited by 8 publications

References 55 publications

How Does the Spatial Confinement of FtsZ to a Membrane Surface Affect Its Polymerization Properties and Function?

How Does the Spatial Confinement of FtsZ to a Membrane Surface Affect Its Polymerization Properties and Function?

Kinetics of Single-Enzyme Reactions on Vesicles: Role of Substrate Aggregation

Micro-mechanical, continuum-mechanical, and AFM-based descriptions of elasticity in open cylindrical micellar filaments

Contact Info

Product

Resources

About