Abstract
Abstract
Phospholipases A2 (PLA2s) catalyze the hydrolysis of glycerophospholipids at the sn-2 position, and their inhibition is considered a rational approach for the prevention and treatment of inflammation. A number of amides and esters of alpha-amino acids with saturated linear side chains, esters of alpha-amino alcohols and derivatives of lipidic peptides were prepared and tested against secreted humal platelet phospholipase A2. Among the compounds tested the amides of free amino acids with long-chain amines presented the highest in vitro inhibitory activity.
Phospholipases A2 (PLA2s) catalyze the hydrolysis of glycerophospholipids at the sn-2 position, and their inhibition is considered a rational approach for the prevention and treatment of inflammation. A number of amides and esters of alpha-amino acids with saturated linear side chains, esters of alpha-amino alcohols and derivatives of lipidic peptides were prepared and tested against secreted humal platelet phospholipase A2. Among the compounds tested the amides of free amino acids with long-chain amines presented the highest in vitro inhibitory activity.
| Original language | English |
|---|---|
| Pages (from-to) | 160-166 |
| Number of pages | 7 |
| Journal | International Journal of Peptide and Protein Research |
| Volume | 48 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 1996 |