Revealing Interfacial Lipid Hydrolysis Catalyzed by Phospholipase A1 at Molecular Level via Sum Frequency Generation Vibrational Spectroscopy and Fluorescence Microscopy
Source abstract
Abstract
The interfacial hydrolysis of phospholipids catalyzed by phospholipase A1 (PLA1) was studied via sum frequency generation (SFG) vibrational spectroscopy and fluorescence microscopy. Both monolayer and bilayer setups were used to confirm the hydrolysis mechanism. During the hydrolysis, lysophospholipids, one of the hydrolysis products, were desorbed from the interface into the solution, while the other products, fatty acids, self-organized and accumulated with PLA1 at the interface to form the PLA1-induced regions, which can serve as nonspecific binding domains for proteins and thus lead to human vascular diseases. This experimental study provides the essential information on revealing the interfacial biochemical process related to the metabolism of the lipids, which is one of the basic building blocks for cells.
Source: openalex_inverted_index · Quality: baseline
Research context
OpenAlex topics: Spectroscopy and Quantum Chemical Studies · Lipid Membrane Structure and Behavior · Photosynthetic Processes and Mechanisms
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
Department of Biomedical Engineering, Southeast University, Nanjing, Jiangsu 210096, China
Institute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Hungarian Academy of Sciences, H-1117 Budapest, Hungary
Funding
Ministry of Education of the People's Republic of China · Ministry of Science and Technology of the People's Republic of China · National Natural Science Foundation of China · Priority Academic Program Development of Jiangsu Higher Education Institutions · National Demonstration Center for Experimental Biomedical Engineering Education, Southeast University
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