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Main Authors: Mak, Claudia A, Chriscoli, Vincent, Lam, Vinson, Yang, Jing, Liu, Lu-Ning, Vecchiarelli, Anthony G
Format: Artículo científico
Language:en
Published: ACS nano 2025
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Online Access:https://pubmed.ncbi.nlm.nih.gov/40163328/
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author Mak, Claudia A
Chriscoli, Vincent
Lam, Vinson
Yang, Jing
Liu, Lu-Ning
Vecchiarelli, Anthony G
author_facet Mak, Claudia A
Chriscoli, Vincent
Lam, Vinson
Yang, Jing
Liu, Lu-Ning
Vecchiarelli, Anthony G
Mak, Claudia A
Chriscoli, Vincent
Lam, Vinson
Yang, Jing
Liu, Lu-Ning
Vecchiarelli, Anthony G
collection PubMed - marine biology
contents Carboxysome Shell Protein CcmK2 Assembles into Monodisperse and pH-Reversible Microparticles. Mak, Claudia A Chriscoli, Vincent Lam, Vinson Yang, Jing Liu, Lu-Ning Vecchiarelli, Anthony G Hydrogen-Ion Concentration Particle Size Bacterial Proteins Synthetic nano- and microparticles have become essential tools in biotechnology. Protein-based compartments offer distinct advantages over synthetic particles, such as biodegradability and biocompatibility, but their development is still in its infancy. Bacterial microcompartments (BMCs) are protein-based organelles consisting of a protein shell encapsulating an enzymatic core. BMCs are self-assembling, selectively permeable, and modular, making them ideal candidates for the development of protein compartments for biotechnology. Indeed, several groups have engineered BMC shells and individual shell proteins into synthetic nanoreactors and functionalized molecular scaffolds. Expanding the variety of architectures assembled from BMC shell proteins will increase their versatility as building blocks in biotechnology. Here, we developed a method for the assembly of single-component monodisperse microparticles using only CcmK2, the major hexameric shell protein of the β-carboxysome BMC. We report the controlled assembly of a single type of BMC shell protein into a solid microparticle. High-resolution imaging revealed CcmK2 particles to be assemblies of radially clustered nanotubes. Through biochemical characterization, we determined the conditions for reversible assembly and residues mediating assembly. We found that pH is a key regulator of final particle size and disassembly. Our study situates CcmK2 particles as precisely controlled and self-assembling monodisperse solid protein particles for future applications in biotechnology.
format Artículo científico
id pubmed_40163328
institution PubMed
language en
publishDate 2025
publisher ACS nano
record_format pubmed
spellingShingle Carboxysome Shell Protein CcmK2 Assembles into Monodisperse and pH-Reversible Microparticles.
Mak, Claudia A
Chriscoli, Vincent
Lam, Vinson
Yang, Jing
Liu, Lu-Ning
Vecchiarelli, Anthony G
Hydrogen-Ion Concentration
Particle Size
Bacterial Proteins
Carboxysome Shell Protein CcmK2 Assembles into Monodisperse and pH-Reversible Microparticles. Mak, Claudia A Chriscoli, Vincent Lam, Vinson Yang, Jing Liu, Lu-Ning Vecchiarelli, Anthony G Hydrogen-Ion Concentration Particle Size Bacterial Proteins Synthetic nano- and microparticles have become essential tools in biotechnology. Protein-based compartments offer distinct advantages over synthetic particles, such as biodegradability and biocompatibility, but their development is still in its infancy. Bacterial microcompartments (BMCs) are protein-based organelles consisting of a protein shell encapsulating an enzymatic core. BMCs are self-assembling, selectively permeable, and modular, making them ideal candidates for the development of protein compartments for biotechnology. Indeed, several groups have engineered BMC shells and individual shell proteins into synthetic nanoreactors and functionalized molecular scaffolds. Expanding the variety of architectures assembled from BMC shell proteins will increase their versatility as building blocks in biotechnology. Here, we developed a method for the assembly of single-component monodisperse microparticles using only CcmK2, the major hexameric shell protein of the β-carboxysome BMC. We report the controlled assembly of a single type of BMC shell protein into a solid microparticle. High-resolution imaging revealed CcmK2 particles to be assemblies of radially clustered nanotubes. Through biochemical characterization, we determined the conditions for reversible assembly and residues mediating assembly. We found that pH is a key regulator of final particle size and disassembly. Our study situates CcmK2 particles as precisely controlled and self-assembling monodisperse solid protein particles for future applications in biotechnology.
title Carboxysome Shell Protein CcmK2 Assembles into Monodisperse and pH-Reversible Microparticles.
topic Hydrogen-Ion Concentration
Particle Size
Bacterial Proteins
url https://pubmed.ncbi.nlm.nih.gov/40163328/