AI Article Synopsis
- Protein amyloid aggregation plays a crucial role in amyloidosis, a group of degenerative diseases, and this study examines how two specific phospholipids (DMPC and DHPC) affect this aggregation process in hen egg white lysozyme.
- Using techniques like fluorescence spectroscopy and atomic force microscopy, the researchers found that these phospholipids can inhibit the formation of lysozyme fibrils in a dose-dependent manner, with DMPC being more effective due to its longer tail structure.
- The study concludes that the inhibition occurs because the phospholipids interfere with essential protein interactions without altering the structure of existing amyloid fibrils, suggesting potential for these phospholipids in modulating amyloid aggregation in related
Article Abstract
Background: Protein amyloid aggregation is an important pathological feature of a group of different degenerative human diseases called amyloidosis. We tested effect of two phospholipids, 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) and 1,2-dihexanoyl-sn-glycero-3-phosphocholine (DHPC) on amyloid aggregation of hen egg white (HEW) lysozyme in vitro.
Methods: Effect of phospholipids was investigated using spectroscopic techniques (fluorescence and CD spectroscopy), atomic force microscopy and image analysis.
Results: Phospholipids DMPC and DHPC are able dose-dependently inhibit lysozyme fibril formation. The length of the phospholipid tails and different structural arrangement of the phospholipid molecules affect inhibitory activity; long-chain DMPC inhibits fibrillization more efficiently. Interestingly, interference of DMPC with lysozyme amyloid fibrils has no effect on their morphology or amount.
Conclusions: Phospholipid molecules have significant effect on lysozyme amyloid fibrillization. We suggest that inhibitory activity is due to the interference of phospholipids with lysozyme leading to the blocking of the intermolecular protein interactions important for formation of the cross-β structure within the core of the fibrils. The higher inhibitory activity of DMPC is probably due to adsorption of protein molecules on the liposome surfaces which caused decrease of species needed for fibrillization. Interaction of the phospholipids with formed fibrils is not sufficient enough to interrupt the bonds in β-sheets which are required for destroying of amyloid fibrils.
General Significance: The obtained results contribute to a better understanding of the effect of phospholipids on amyloid fibrillization of the lysozyme. The data suggest that DMPC and DHPC phospholipids represent agents able to modulate lysozyme amyloid aggregation.
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| http://dx.doi.org/10.1016/j.bbagen.2017.08.023 | DOI Listing |
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