ArticleBiophysical journal2008
Molecular basis of phospholipase A2 activity toward phospholipids with sn-1 substitutions.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- PLAPharmaceutics · 2022Article
- Computational Simulations to Guide Enzyme-Mediated Prodrug Activation.International journal of molecular sciences · 2020Review
- Molecular Modeling-Guided Design of Phospholipid-Based Prodrugs.International journal of molecular sciences · 2019Article
- Prospects and Challenges of Phospholipid-Based Prodrugs.Pharmaceutics · 2018Article
- Metabolic profiling reveals that PNPLA3 induces widespread effects on metabolism beyond triacylglycerol remodeling in Huh-7 hepatoma cells.American journal of physiology. Gastrointestinal and liver physiology · 2014Article
- Synthesis of phospholipids on a glyceric acid scaffold: design and preparation of phospholipase ATetrahedron · 2014Article
- Surface dilution kinetics of phospholipase A(2) catalyzed lipid-bilayer hydrolysis.The journal of physical chemistry. B · 2014Article
- Quercetin modulates activities of Taiwan cobra phospholipase A2 via its effects on membrane structure and membrane-bound mode of phospholipase A2.Journal of biosciences · 2012Article
- Study of Thermomyces lanuginosa lipase in the presence of tributyrylglycerol and water.Biophysical journal · 2009Article
- Phospholipase A2 biochemistry.Cardiovascular drugs and therapy · 2009Review
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We studied secretory phospholipase A(2) type IIA (sPLA(2)) activity toward phospholipids that are derivatized in the sn-1 position of the glycerol backbone. We explored what type of side group (small versus bulky groups, hydrophobic versus polar groups) can be introduced at the sn-1 position of the glycerol backbone of glycerophospholipids and at the same time be hydrolyzed by sPLA(2). The biophysical characterization revealed that the modified phospholipids can form multilamellar vesicles, and several of the synthesized sn-1 functionalized phospholipids were hydrolyzed by sPLA(2). Molecular dynamics simulations provided detailed insight on an atomic level that can explain the observed sPLA(2) activity toward the different phospholipid analogs. The simulations revealed that, depending on the nature of the side chain located at the sn-1 position, the group may interfere with an incoming water molecule that acts as the nucleophile in the enzymatic reaction. The simulation results are in agreement with the experimentally observed sPLA(2) activity toward the different phospholipid analogs.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.