Phase-Dependent Adsorption of Myelin Basic Protein to Phosphatidylcholine Lipid Bilayers
| Autor: | Petra Maleš, Zlatko Brkljača, Ivo Crnolatac, Dražen Petrov, Danijela Bakarić |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2024 |
| Předmět: |
myelin basic protein (MBP)
1 2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) lipid phase-dependent hydration of MBP hydrophobic amino acids spectroscopic (UV-Vis FTIR CD) and calorimetric (DSC) measurements molecular dynamics (MD) simulations Chemical technology TP1-1185 Chemical engineering TP155-156 |
| Zdroj: | Membranes, Vol 14, Iss 1, p 15 (2024) |
| Druh dokumentu: | article |
| ISSN: | 2077-0375 |
| DOI: | 10.3390/membranes14010015 |
| Popis: | The dense packing of opposite cytoplasmic surfaces of the lipid-enriched myelin membrane, responsible for the proper saltatory conduction of nerve impulses through axons, is ensured by the adhesive properties of myelin basic protein (MBP). Although preferentially interacting with negatively charged phosphatidylserine (PS) lipids, as an intrinsically disordered protein, it can easily adapt its shape to its immediate environment and thus adsorb to domains made of zwitterionic phosphatidylcholine (PC) lipids. As the molecular-level interaction pattern between MBP and PC lipid membranes suffers from scarce characterization, an experimental and computational study of multilamellar liposomes (MLVs) composed of 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) in the presence of bovine MBP is presented here. Calorimetric and temperature-dependent UV-Vis measurements identified DPPC pretransition temperature (Tp) and calorimetric enthalpy (ΔHcal) as the physicochemical parameters most responsive to the presence of MBP. Besides suggesting an increase in β-sheet fractions of structured MBP segments as DPPC lipids undergo from the gel (20 °C) to the fluid (50 °C) phase, FTIR spectra unraveled the significant contribution of lysine (Lys) residues in the adsorption pattern, especially when DPPC is in the fluid (50 °C) phase. In addition to highlighting the importance of Lys residues in the MBP adsorption on DPPC lipid bilayer, employing salt bridges (SBs) and hydrogen bonds (HBs), MD data suggest the crucial importance of the orientation of MBP with respect to the surface of the DPPC lipid bilayer. |
| Databáze: | Directory of Open Access Journals |
| Externí odkaz: |
|
| Nepřihlášeným uživatelům se plný text nezobrazuje | K zobrazení výsledku je třeba se přihlásit. |