Contribution to a conference proceedings/Contribution to a book

FZJ-2020-01420

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Solvent Effects on the Binding of Fatty Acids to Human Serum Albumin

Pant, P. ; Ruiz-Blanco, Y. B. ; Sanchez-Garcia, E. (Corresponding author)

2020
Forschungszentrum Jülich GmbH Zentralbibliothek, Verlag Jülich

Please use a persistent id in citations: http://hdl.handle.net/2128/24519

Abstract: Solvent interactions can influence the properties and function of complex biomolecules. Among others, altering the solvent composition has consequences for the recognition of binding partners. Human serum albumin (HSA) is one of the most enigmatic biomolecules, known as an efficient carrier of biological materials, such as hormones, fatty acids and drugs. Here we explored the effects of the solvent on stearic acid-HSA binding. To this end, we performed all-atom molecular dynamics (MD) simulations in explicit solvent (~ 2.9 μs in total). These MD simulations were carried out in explicit water and in a 20% ethanol-water mixture. The sampling in both systems was processed with the MM-PBSA binding free energy approach, which allowed us to investigate the effects of the solvent composition on the binding of stearic acid molecules to seven binding sites of HSA. Using this computational approach, we were able to reproduce the experimental preference of fatty acid’s binding sites for albumin in water. Site 5 > site 4 > site 2 were calculated as high affinity fatty acid binding sites, in agreement with the experimental reports.[1] Interestingly, we observed that site 1 becomes the most prominent binding pocket in the 20% ethanol-water mixture, with overall binding affinity towards stearic acid: site 1 > site 5 > site 2. Our simulations in explicit solvent also provided a rationale for this effect. Importantly, we achieved weak binding-to strong binding conversion by using a solvent mixture, with repercussions for the specific binding properties and the manipulation of HSA properties as biological carrier.

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Contributing Institute(s):

1. John von Neumann - Institut für Computing (NIC)

Research Program(s):

1. 899 - ohne Topic (POF3-899) (POF3-899)

Appears in the scientific report 2020

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Linked articles:

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Book/Proceedings Müller, M. (Editor)Extern* ; Binder, K. (Editor) ; Trautmann, A. (Editor)FZJ*
NIC Symposium 2020: proceedings
2020NIC Symposium, JülichJülich, Germany, 27 Feb 2020 - 28 Feb 20202020-02-272020-02-28 Jülich : Forschungszentrum Jülich GmbH Zentralbibliothek, Verlag, NIC Series 50, v, 424 S. (2020)2020   Files  Fulltext by OpenAccess repository BibTeX | EndNote: XML, Text | RIS

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