Influence of the surrounding environment in re-naturalized β-barrel membrane proteins
| Autor: | Maximilien Lopes-Rodrigues, David Zanuy, Carlos Alemán, Juan Torras, Catherine Michaux, Eric A. Perpète, Jordi Triguero |
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| Přispěvatelé: | Universitat Politècnica de Catalunya. Departament d'Enginyeria Química, Universitat Politècnica de Catalunya. IMEM - Innovació, Modelització i Enginyeria en (BIO) Materials |
| Jazyk: | angličtina |
| Rok vydání: | 2018 |
| Předmět: |
Models
Molecular 0301 basic medicine Detergents Lipid Bilayers Bioinspired membrane Biophysics Porins Molecular Dynamics Simulation Molecular dynamics 010402 general chemistry 01 natural sciences Biochemistry Lipid bilayer 03 medical and health sciences Enginyeria química [Àrees temàtiques de la UPC] Membrane proteins Dinàmica molecular Micelles Ion transporter Detergent bilayer Aqueous solution Chemistry Bilayer Organic Chemistry Proteïnes de membrana Water Hydrogen-Ion Concentration biochemical phenomena metabolism and nutrition 0104 chemical sciences 030104 developmental biology Membrane Critical micelle concentration Membrane protein Porin bacteria |
| Zdroj: | Lopes Rodrigues, M, Triguero, J, Torras, J, Perpète, E, Michaux, C, Zanuy, D & Aleman, C 2018, ' Influence of the surrounding environment in re-naturalized β-barrel membrane proteins. ', Biophysical chemistry, vol. 234, pp. 6-15 . https://doi.org/10.1016/j.bpc.2017.12.003 UPCommons. Portal del coneixement obert de la UPC Universitat Politècnica de Catalunya (UPC) Recercat. Dipósit de la Recerca de Catalunya instname |
| Popis: | © 2017 Elsevier B.V. Outer-membrane porins are currently being used to prepare bioinspired nanomembranes for selective ion transport by immobilizing them into polymeric matrices. However, the fabrication of these protein-integrated devices has been found to be strongly influenced by the instability of the ß-barrel porin structure, which depends on surrounding environment. In this work, molecular dynamics simulations have been used to investigate the structural stability of a representative porin, OmpF, in three different environments: (i) aqueous solution at pH = 7; (ii) a solution of neutral detergent in a concentration similar to the critical micelle concentration; and (iii) the protein embedded into a neutral detergent bilayer. The results indicate that the surrounding environment not only alters the stability of the ß-barrel but affects the internal loop responsible of the ions transport, as well as the tendency of the porin proteins to aggregate into trimers. The detergent bilayer preserves the structure of OmpF protein as is found bacteria membranes, while pure aqueous solution induces a strong destabilization of the protein. An intermediate situation occurs for detergent solution. Our results have been rationalized in terms of protein ¿ water and protein ¿ detergent interactions, which makes them extremely useful for the future design of new generation of bioinspired protein-integrated devices. |
| Databáze: | OpenAIRE |
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