ArticleThe journal of physical chemistry. B2014
Role of anisotropic interactions for proteins and patchy nanoparticles.
Article in The journal of physical chemistry. B, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Review
- Interplay of Hydrophobicity, Charge, and Sequence Length in Oligopeptide Coassembly.The journal of physical chemistry. B · 2025Article
- Protein and Peptide Therapeutics: Stability Challenges, Regulatory Demands, and Innovative Formulation Solutions for Enhanced Clinical Effectiveness.Protein and peptide letters · 2025Review
- Role of Domain-Domain Interactions on the Self-Association and Physical Stability of Monoclonal Antibodies: Effect of pH and Salt.The journal of physical chemistry. B · 2023Article
- ATP and Tri-Polyphosphate (TPP) Suppress Protein Aggregate Growth by a Supercharging Mechanism.Biomedicines · 2021Article
- Multiscale Coarse-Grained Approach to Investigate Self-Association of Antibodies.Biophysical journal · 2020Article
- Dynamics of liquid-liquid phase separation of wheat gliadins.Scientific reports · 2018Article
- In Silico Prediction of Diffusion Interaction Parameter (kPharmaceutical research · 2018Article
- Self-association of a highly charged arginine-rich cell-penetrating peptide.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Charge Shielding Prevents Aggregation of Supercharged GFP Variants at High Protein Concentration.Molecular pharmaceutics · 2017Article
- Contrasting the Influence of Cationic Amino Acids on the Viscosity and Stability of a Highly Concentrated Monoclonal Antibody.Pharmaceutical research · 2017Article
- Effect of the surface charge distribution on the fluid phase behavior of charged colloids and proteins.The Journal of chemical physics · 2016Article
- Modulating non-native aggregation and electrostatic protein-protein interactions with computationally designed single-point mutations.Protein engineering, design & selection : PEDS · 2016Article
- Coupling of isotropic and directional interactions and its effect on phase separation and self-assembly.The Journal of chemical physics · 2016Article
- Review
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Authors and funding
2 authors.
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Abstract
Protein-protein interactions are inherently anisotropic to some degree, with orientation-dependent interactions between repulsive and attractive or complementary regions or "patches" on adjacent proteins. In some cases it has been suggested that such patch-patch interactions dominate the thermodynamics of dilute protein solutions, as captured by the osmotic second virial coefficient (B22), but delineating when this will or will not be the case remains an open question. A series of simplified but exactly solvable models are first used to illustrate that a delicate balance exists between the strength of attractive patch-patch interactions and the patch size, and that repulsive patch-patch interactions contribute significantly to B22 for only those conditions where the repulsions are long-ranged. Finally, B22 is reformulated, without approximations, in terms of the density of states for a given interaction energy and particle-particle distance. Doing so illustrates the inherent balance of entropic and energetic contributions to B22. It highlights that simply having strong patch-patch interactions will only cause anisotropic interactions to dominate B22 solution properties if the unavoidable entropic penalties are overcome, which cannot occur if patches are too small. The results also indicate that the temperature dependence of B22 may be a simple experimental means to assess whether a small number of strongly attractive configurations dominate the dilute solution behavior.
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