Molecular basis of phospholipase A2 activity toward phospholipids with sn-1 substitutions.

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 t

SUBMITTER: Linderoth L 

PROVIDER: S-EPMC2134884 | biostudies-literature | 2008 Jan

REPOSITORIES: biostudies-literature