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Carrillo, J.-M.

Publications and source records attributed to Carrillo, J.-M..

2 recordsLinked to original sources

Effects of central dogma processes on the compaction and segregation of bacterial nucleoids

The bacterial cytoplasm is characterized by a distinctive membrane-less organelle, the nucleoid, which harbors chromosomal DNA. We investigate the effects of dynamic processes associated with transcription and translation on the structure of this organelle, using coarsegrained molecular dynamics (MD) simulations implemented with out-of-equilibrium reactions. Our model captures the scale of the entire cell and incorporates a reaction-diffusion system for ribosomes and polyribosomes, combining their out-of-equilibrium dynamics with excluded volume interactions with DNA. Our findings demonstrate that out-of-equilibrium reactions increase the size of the nucleoid. In addition, we show that the nucleoid size increase is proportional to transcriptional activity. Our model reproduces the time-dependent change in nucleoid size observed in rifampicin treatment experiments, where the pool of polyribosomes is depleted. Furthermore, we find these active processes are essential for complete sister chromosome separation and correct nucleoid positioning within the cell. Overall, our study reveals the effects of the central dogma processes on the internal organization and localization of bacterial nucleoids. SignificanceUnderstanding how bacteria organize their chromosomes is fundamental to cell biology. Through our coarse-grained molecular dynamics simulations incorporating out-of-equilibrium processes of transcription and translation, we are able to capture the effects of these central dogma processes on DNA organization and demonstrate that these active biological processes expand the nucleoid and facilitate the separation of daughter chromosomes. Our simulations are compared to experimental measurements and highlight the impact of the out-of-equilibrium conditions of the living cell. These findings point out the crucial interplay between physical forces and biological activity in cellular organization, suggesting that cellular structure depends on non-equilibrium processes.

biophysics↗

All-Atom Modeling and Simulation of Biopolymer Interface: Dual Role of Antifouling Polymer Brushes

Antifouling polymers are highly valuable in a variety of applications, including antiviral coatings, targeted drug delivery, and marine coatings, where preventing unwanted protein adsorption is critical. Although extensive experimental studies have characterized polymer-protein interactions, computational studies remain limited due to the inherent difficulty of modeling and integrating these distinct components within a unified system. This study presents molecular modeling and simulation of polyelectrolyte and polyzwitterionic brushes--poly(dimethylaminoethyl methacrylate) (PDMAEMA), poly(2-(N-oxide-N,N-dimethylamino)ethyl methacrylate) (PNOMA), and poly(2-(N-3-sulfopropyl-N,N-dimethylammonium)ethyl methacrylate) (PSBMA)--grafted onto -quartz substrates in the presence of lysozyme protein. The brush models were developed to closely replicate experimentally synthesized brush samples and to provide detailed insights into structural and dynamical changes at the molecular level during protein adsorption. Using steered molecular dynamics simulations, we show that the PSBMA brush, due to its high local density, exhibits the greatest resistance to protein insertion. C root-mean-square deviation and interaction patterns analyses further reveal that PSBMA also induces the most significant destabilization of lysozyme, while PDMAEMA brush enhances protein stability through ion-mediated interactions. The PNOMA brush, while requiring the lowest force for protein adsorption, induces greater protein destabilization than the PDMAEMA brush primarily due to electrostatic repulsion caused by a short carbon spacer length. To the best of our knowledge, this study presents the first comprehensive and realistic model system--comprising nanomaterials, polymers, and proteins, specifically antifouling polyzwitterions and polyelectrolytes grafted onto -quartz substrates via linkers. These findings highlight the dual role of antifouling polymer brushes: resisting protein adsorption and modulating protein structural dynamics, offering valuable insights for the rational design of next-generation antifouling materials. TOC GRAPHICS O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=181 SRC="FIGDIR/small/651893v1_ufig1.gif" ALT="Figure 1"> View larger version (72K): org.highwire.dtl.DTLVardef@9620b8org.highwire.dtl.DTLVardef@3e395dorg.highwire.dtl.DTLVardef@1282169org.highwire.dtl.DTLVardef@1a997f7_HPS_FORMAT_FIGEXP M_FIG C_FIG

bioengineering↗