Version 1
: Received: 31 October 2024 / Approved: 1 November 2024 / Online: 5 November 2024 (04:15:07 CET)
How to cite:
Przybyłek, M.; Bełdowski, P.; Ledziński, D.; Lutowski, Z.; Mazurkiewicz, A.; Raczyński, P.; Dedinaite, A.; Claesson, P. M. Molecular Insights into the Interactions Between Human Serum Albumin and Phospholipid Membranes. Preprints2024, 2024110036. https://doi.org/10.20944/preprints202411.0036.v1
Przybyłek, M.; Bełdowski, P.; Ledziński, D.; Lutowski, Z.; Mazurkiewicz, A.; Raczyński, P.; Dedinaite, A.; Claesson, P. M. Molecular Insights into the Interactions Between Human Serum Albumin and Phospholipid Membranes. Preprints 2024, 2024110036. https://doi.org/10.20944/preprints202411.0036.v1
Przybyłek, M.; Bełdowski, P.; Ledziński, D.; Lutowski, Z.; Mazurkiewicz, A.; Raczyński, P.; Dedinaite, A.; Claesson, P. M. Molecular Insights into the Interactions Between Human Serum Albumin and Phospholipid Membranes. Preprints2024, 2024110036. https://doi.org/10.20944/preprints202411.0036.v1
APA Style
Przybyłek, M., Bełdowski, P., Ledziński, D., Lutowski, Z., Mazurkiewicz, A., Raczyński, P., Dedinaite, A., & Claesson, P. M. (2024). Molecular Insights into the Interactions Between Human Serum Albumin and Phospholipid Membranes. Preprints. https://doi.org/10.20944/preprints202411.0036.v1
Chicago/Turabian Style
Przybyłek, M., Andra Dedinaite and Per M. Claesson. 2024 "Molecular Insights into the Interactions Between Human Serum Albumin and Phospholipid Membranes" Preprints. https://doi.org/10.20944/preprints202411.0036.v1
Abstract
In this study, molecular dynamics simulations were employed to analyze interactions between phospholipid membranes and human serum albumin (HSA) in the presence of mono- and divalent cations. Two types of membranes, composed of dipalmitoyl phosphatidylcholine (DPPC) and dipalmitoyl phosphatidylethanolamine (DPPE), were utilized. The results revealed that both systems exhibited high stability, with the DPPE complexes displaying greater stability compared to those formed with DPPC. This increased stability was attributed to a higher number of ionic contacts and hydrogen bonds. The presence of mono- and divalent metal cations significantly influenced the membrane’s capacity to bind proteins. However, these effects varied depending on the phospholipid composition of the bilayer. The studies confirmed the relatively low ability of DPPC to bind potassium ions, as previously observed by others. Consequently, the DPPC/HSA/K+ complex was found to be the least stable among the systems studied. While DPPC interactions were limited to HSA domains I and II, DPPE was able to interact with all domains of the protein. Both lipid bilayers exhibited substantial structural changes and characteristic curvature induced by interactions with HSA, which confirms the formation of relatively strong interactions capable of influencing the arrangement of the phospholipids.
Keywords
phospholipid membranes; DPPC; DPPE; human serum albumin; intermolecular interactions; hydrogen bonds; ionic interactions; mono- and divalent cations; molecular dynamics
Subject
Chemistry and Materials Science, Theoretical Chemistry
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
