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Biological molecules self-assemble into huge functional structures by striking a delicate balance between electrical and hydrophobic forces. Both factors must be understood in order to comprehend the process of protein self-assembly. Hydrophobic interactions of proteins are more difficult to anticipate than their electrical counterparts.
Proteins align into membrane-like structures through hydrophobic interactions, as explained in a study by Angel Mozo-Villarias and colleagues from the Autonoma University of Barcelona, Spain, and published in The European Physical Journal E. The model has the potential to be used as a tool in the discovery of new materials and therapeutics by assisting in the prediction of the structure of macromolecular assemblies at any length scale.
Hydrophobicity is not a property of individual molecule but rather an emergent trait of large molecular systems. It is measured by the amount of energy required to transfer an amino acid from a hydrophilic medium to a hydrophobic one, and this is how scientists analyze proteins. These indexes—the “hydrophobic charges”—establish a hydrophobic field for a set of amino acids, analogous to how a distribution of electrical charges generates an electric field.
Mozo-Villarias and colleagues initially established a vector that described the dipolar nature of a protein based on the distribution of hydrophobic charges on the protein. The energy stored in a system made up of two hydrophobic dipoles was then computed using an electrical analogy. Hydrophobic dipoles were shown to align parallel to one other in simulations, much like phospholipid molecules in biological membranes tend to arrange themselves to form a double layer.
The membrane effect is a hydrophobic mechanism for self-assembling proteins to align before forming stable interactions. The team concludes that effect is a universal concept responsible for nature’s rich diversity of protein assembly morphologies.
Sources:
Juan A. Cedano et al. (2023). How hydrophobicity shapes the architecture of protein assemblies, The European Physical Journal E. DOI: 10.1140/epje/s10189-023-00320-8
https://phys.org/news/2023-09-hydrophobicity-protein.html
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Keywords: protein assembly, protein structure
