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Palmitoylation modifies transmembrane adaptor protein PAG for ordered lipid environment: A molecular dynamics simulation study
- 1.0578225 - ÚFCH JH 2025 RIV NL eng J - Journal Article
Saija, Maria Chiara - Melcrová, Adéla - Pajerski, Wojciech - Schachter, I. - Javanainen, M. - Cebecauer, Marek - Cwiklik, Lukasz
Palmitoylation modifies transmembrane adaptor protein PAG for ordered lipid environment: A molecular dynamics simulation study.
Biophysical Chemistry. Roč. 304, JAN 2024 (2024), č. článku 107124. ISSN 0301-4622. E-ISSN 1873-4200
R&D Projects: GA ČR(CZ) GX19-26854X
Institutional support: RVO:61388955
Keywords : PAG * membranes * Palmitoylation
OECD category: Physical chemistry
Impact factor: 3.8, year: 2022
Method of publishing: Limited access
https://www.sciencedirect.com/science/article/pii/S0301462223001758
We employed all-atom MD simulations to investigate the impact of palmitoylation on the PAG transmembrane peptide within various lipid environments, including the less explored boundary region separating lipid-ordered (Lo) and lipid-disordered (Ld) membrane phases. We found that palmitoylation of the peptide reduces its impact on membrane thickness, particularly within the Lo and boundary environments. Despite their hydrophobic nature, the palmitoyl chains on the peptide did not significantly affect the hydration of the surrounding membrane. Interestingly, the boundary membrane environment was found to be especially compatible with the palmitoylated peptide, suggesting its potential for accumulation in phase boundaries. Our findings highlight the importance of understanding how palmitoylation-modified peptides behave within membranes, with crucial implications for cell signaling and membrane organization. This knowledge may also inform the optimization of lipid membrane-based drug delivery systems, by improving our understanding of how drugs and excipients can be most effectively arranged within these carriers.
Permanent Link: https://hdl.handle.net/11104/0347250
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