How hydrophobicity shapes the architecture of protein assemblies
Cedano Rodríguez, Juan Antonio (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Querol Murillo, Enrique (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Mozo-Villarias, Angel (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)

Data:	2023
Resum:	The interactions that give rise to protein self-assembly are basically electrical and hydrophobic in origin. The electrical interactions are approached in this study as the interaction between electrostatic dipoles originated by the asymmetric distribution of their charged amino acids. However, hydrophobicity is not easily derivable from basic physicochemical principles. Its treatment is carried out here considering a hydrophobic force field originated by "hydrophobic charges". These charges are indices obtained experimentally from the free energies of transferring amino acids from polar to hydrophobic media. Hydrophobic dipole moments are used here in a manner analogous to electric dipole moments, and an empirical expression of interaction energy between hydrophobic dipoles is derived. This methodology is used with two examples of self-assembly systems of different complexity. It was found that the hydrophobic dipole moments of proteins tend to interact in such a way that they align parallel to each other in a completely analogous way to how phospholipids are oriented in biological membranes to form the well-known double layer. In this biological membrane model (BM model), proteins tend to interact in a similar way, although in this case this alignment is modulated by the tendency of the corresponding electrostatic dipoles to counter-align.
Ajuts:	Agencia Estatal de Investigación BIO2017-84166R Agencia Estatal de Investigación PID2021-125632OB-C22
Nota:	Altres ajuts: acords transformatius de la UAB
Drets:	Aquest document està subjecte a una llicència d'ús Creative Commons. Es permet la reproducció total o parcial, la distribució, la comunicació pública de l'obra i la creació d'obres derivades, fins i tot amb finalitats comercials, sempre i quan es reconegui l'autoria de l'obra original.
Llengua:	Anglès
Document:	Article ; recerca ; Versió publicada
Publicat a:	The European Physical Journal. E, Soft Matter, Vol. 46 (July 2023) , art. 62, ISSN 1292-895X

DOI: 10.1140/epje/s10189-023-00320-8
PMID: 37495860

10 p, 2.0 MB

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