ArticleThe journal of physical chemistry. B2019
Elucidating the Thermodynamic Driving Forces of Polyanion-Templated Virus-like Particle Assembly.
Article in The journal of physical chemistry. B, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 22 citations in OpenAlex.
- Molecular biophysics of viral proteins: From mechanistic insights to microbiological and clinical applications.AIMS microbiology · 2026Review
- Pleomorphism in Wild-Type and Engineered PP7 Virus-Like Particles.Small (Weinheim an der Bergstrasse, Germany) · 2025Article
- Furan-rich, biobased transfection agents as potential oligomeric candidates for intracellular plasmid DNA delivery.RSC advances · 2024Article
- Tunable Nanomaterials of Intracellular Crystallization for In Situ Biolabeling and Biomedical Imaging.Chemical & biomedical imaging · 2023Review
- The SARS-CoV-2 Hydra, a tiny monster from the 21st century: Thermodynamics of the BA.5.2 and BF.7 variants.Microbial risk analysis · 2023Article
- Review
- Polyelectrolyte Encapsulation and Confinement within Protein Cage-Inspired Nanocompartments.Pharmaceutics · 2021Review
- Relationships between RNA topology and nucleocapsid structure in a model icosahedral virus.Biophysical journal · 2021Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A virus in its most simple form is comprised of a protein capsid that surrounds and protects the viral genome. The self-assembly of such structures, however, is a highly complex, multiprotein, multiinteraction process and has been a topic of study for a number of years. This self-assembly process is driven by the (mainly electrostatic) interaction between the capsid proteins (CPs) and the genome as well as by the protein-protein interactions, which primarily rely on hydrophobic interactions. Insight in the thermodynamics that is involved in virus and virus-like particle (VLP) formation is crucial in the detailed understanding of this complex assembly process. Therefore, we studied the assembly of CPs of the cowpea chlorotic mottle virus (CCMV) templated by polyanionic species (cargo), that is, single-stranded DNA (ssDNA), and polystyrene sulfonate (PSS) using isothermal titration calorimetry. By separating the electrostatic CP-cargo interaction from the full assembly interaction, we conclude that CP-CP interactions cause an enthalpy change of -3 to -4 kcal mol
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.