ArticleBiophysical journal2011
Effects of macromolecular crowding on the inhibition of virus assembly and virus-cell receptor recognition.
Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 23 citations in OpenAlex.
- Effects of Molecular Crowding on the Structural, Dynamic, and Functional Properties of Biological Macromolecules: A General Overview.Sub-cellular biochemistry · 2025Review
- Allosteric HIV Integrase Inhibitors Promote Formation of Inactive Branched Polymers via Homomeric Carboxy-Terminal Domain Interactions.Structure (London, England : 1993) · 2021Article
- Virus Mechanics under Molecular Crowding.The journal of physical chemistry. B · 2021Article
- What macromolecular crowding can do to a protein.International journal of molecular sciences · 2014Review
- Applying molecular crowding models to simulations of virus capsid assembly in vitro.Biophysical journal · 2014Article
- Article
- Influence of crowded cellular environments on protein folding, binding, and oligomerization: biological consequences and potentials of atomistic modeling.FEBS letters · 2013Review
- Association equilibrium of the HIV-1 capsid protein in a crowded medium reveals that hexamerization during capsid assembly requires a functional C-domain dimerization interface.Biophysical journal · 2013Article
- A physics-based approach of coarse-graining the cytoplasm of Escherichia coli (CGCYTO).Biophysical journal · 2012Article
- Finding a needle in a haystack: the role of electrostatics in target lipid recognition by PH domains.PLoS computational biology · 2012Article
- Rationally designed interfacial peptides are efficient in vitro inhibitors of HIV-1 capsid assembly with antiviral activity.PloS one · 2011Article
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Biological fluids contain a very high total concentration of macromolecules that leads to volume exclusion by one molecule to another. Theory and experiment have shown that this condition, termed macromolecular crowding, can have significant effects on molecular recognition. However, the influence of molecular crowding on recognition events involving virus particles, and their inhibition by antiviral compounds, is virtually unexplored. Among these processes, capsid self-assembly during viral morphogenesis and capsid-cell receptor recognition during virus entry into cells are receiving increasing attention as targets for the development of new antiviral drugs. In this study, we have analyzed the effect of macromolecular crowding on the inhibition of these two processes by peptides. Macromolecular crowding led to a significant reduction in the inhibitory activity of: 1), a capsid-binding peptide and a small capsid protein domain that interfere with assembly of the human immunodeficiency virus capsid, and 2), a RGD-containing peptide able to block the interaction between foot-and-mouth disease virus and receptor molecules on the host cell membrane (in this case, the effect was dependent on the conditions used). The results, discussed in the light of macromolecular crowding theory, are relevant for a quantitative understanding of molecular recognition processes during virus infection and its inhibition.
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