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1.
Sci Rep ; 14(1): 15118, 2024 07 02.
Article in English | MEDLINE | ID: mdl-38956171

ABSTRACT

The use of novel active ingredients for the functional modification of chitosan nanoformulations has attracted global attention. In this study, chitosan has been functionalized via histidine to craft novel chitosan-histidine nanoformulation (C-H NF) using ionic gelation method. C-H NF exhibited elite physico-biochemical properties, influencing physiological and biochemical dynamics in Tomato. These elite properties include homogenous-sized nanoparticles (314.4 nm), lower PDI (0.218), viscosity (1.43 Cps), higher zeta potential (11.2 mV), nanoparticle concentration/ml (3.53 × 108), conductivity (0.046 mS/cm), encapsulation efficiency (53%), loading capacity (24%) and yield (32.17%). FTIR spectroscopy revealed histidine interaction with C-H NF, while SEM and TEM exposed its porous structure. Application of C-H NF to Tomato seedling and potted plants through seed treatment and foliar spray positively impacts growth parameters, antioxidant-defense enzyme activities, reactive oxygen species (ROS) content, and chlorophyll and nitrogen content. We claim that the histidine-functionalized chitosan nanoformulation enhances physico-biochemical properties, highlighting its potential to elevate biochemical and physiological processes of Tomato plant.


Subject(s)
Chitosan , Histidine , Nanoparticles , Solanum lycopersicum , Solanum lycopersicum/metabolism , Solanum lycopersicum/growth & development , Chitosan/chemistry , Histidine/chemistry , Nanoparticles/chemistry , Reactive Oxygen Species/metabolism , Antioxidants/chemistry , Antioxidants/pharmacology , Chlorophyll/metabolism , Chlorophyll/chemistry , Seedlings/growth & development , Seedlings/drug effects , Seedlings/metabolism , Spectroscopy, Fourier Transform Infrared
2.
Biophys J ; 121(12): 2398-2410, 2022 06 21.
Article in English | MEDLINE | ID: mdl-35596527

ABSTRACT

Quorum sensing is a bacterial cell-cell communication process that regulates gene expression. The search and binding of the autoinducer molecule (AHL)-bound LuxR-type proteins to specific sites on DNA in quorum-sensing cells in Gram-negative bacteria is a complex process and has been theoretically investigated based on a discrete-state stochastic approach. It is shown that several factors such as the rate of formation of the AHL-bound LuxR protein within the cells and its dissociation to freely diffusing AHL, the diffusion of the latter in and out of the cells, positive feedback loops, and the cell population density play important roles in the protein target search and can control the gene regulation processes. Physical-chemical arguments to explain these observations are presented. Our calculations of the dynamic properties are also supplemented by Monte Carlo computer simulations. Our theoretical model provides physical insights into the complex mechanisms of protein target search in quorum-sensing cells.


Subject(s)
Acyl-Butyrolactones , Quorum Sensing , Acyl-Butyrolactones/metabolism , Bacterial Proteins/metabolism , DNA , Gene Expression Regulation, Bacterial , Repressor Proteins/metabolism , Trans-Activators/chemistry
3.
J Phys Chem B ; 125(17): 4536-4545, 2021 05 06.
Article in English | MEDLINE | ID: mdl-33900087

ABSTRACT

Transition paths refer to the time taken by molecules to cross a barrier separating two molecular conformations. In this work, we study how memory, as well as inertial contribution in the dynamics along a reaction coordinate, can affect the distribution of the transition-path time. We use a simple model of dynamics governed by a generalized Langevin equation with a power-law memory along with the inertial term, which was neglected in previous studies, where memory effects were explored only in the overdamped limit. We derive an approximate expression for the transit-time distribution and discuss our results for the short- and long-time limits and also compare it with known results in the high friction (overdamped) limit as well as in the Markovian limit. We have developed a numerical algorithm to test our theoretical results against extensive numerical simulations.

4.
J Phys Chem B ; 124(17): 3518-3526, 2020 04 30.
Article in English | MEDLINE | ID: mdl-32268727

ABSTRACT

Protein-DNA interactions are important for all biological processes and involve the process of proteins searching for and recognizing specific binding sites on the DNA. Many aspects of the mechanism of the protein search for targets on DNA are not well understood. One important problem is the effect of DNA conformation on the protein search dynamics. Using a theoretical method based on a discrete-state stochastic approach, we obtained an analytical description of the dynamic properties. We investigated a system with two DNA conformers. It was found that the average search time on one DNA conformer via 1D or 3D motions depended on the dynamics of the search process on the other DNA conformer.


Subject(s)
DNA , Proteins , DNA/metabolism , Monte Carlo Method , Nucleic Acid Conformation , Protein Binding , Protein Conformation , Proteins/metabolism
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