| Autor: | Theodore A. Macrides, George Kweifio-Okai, Lynn D. Hodges |
|---|---|
| Rok vydání: | 2003 |
| Předmět: |
Protease
Tetrapeptide biology medicine.drug_class Stereochemistry medicine.medical_treatment Clinical Biochemistry Substrate (chemistry) Mixed inhibition Cell Biology General Medicine Anti-inflammatory chemistry.chemical_compound chemistry Biochemistry medicine biology.protein Bovine serum albumin Molecular Biology Pancreatic elastase Lupeol |
| Zdroj: | Molecular and Cellular Biochemistry. 252:97-101 |
| ISSN: | 0300-8177 |
| DOI: | 10.1023/a:1025569805468 |
| Popis: | Lupeol-3-palmitate (LP) and lupeol-3-linoleate (LL), two synthetic long chain fatty acid ester analogues of the plant-derived anti-inflammatory pentacyclic triterpenoid lupeol (L), were studied in vitro as potential inhibitors of serine protease activity. With respect to the natural protein substrate bovine serum albumin (BSA), lupeol palmitate and lupeol linoleate inhibited trypsin activity in a manner consistent with mixed inhibition (KIC values of 103 and 52 μM respectively; KIU values of 30 and 14 μM respectively). However, the lupeol esters showed no inhibitory effect on the catalytic activity of porcine pancreatic elastase (PPE) with respect to the synthetic tetrapeptide substrate succinyl-(alanyl)3-p-nitroanilide (SAAANA). The present paper shows the lupeol triterpenes to be selective protease inhibitors. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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