Unusual activity pattern of leucine aminopeptidase inhibitors based on phosphorus containing derivatives of methionine and norleucine
Jazyk angličtina Země Velká Británie, Anglie Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
- MeSH
- aktivace enzymů účinky léků MeSH
- fosfor chemie MeSH
- inhibitory enzymů farmakologie MeSH
- ledviny enzymologie MeSH
- leucylaminopeptidasa antagonisté a inhibitory MeSH
- methionin * chemie farmakologie MeSH
- molekulární struktura MeSH
- norleucin * chemie farmakologie MeSH
- prasata MeSH
- zvířata MeSH
- Check Tag
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- fosfor MeSH
- inhibitory enzymů MeSH
- leucylaminopeptidasa MeSH
- methionin * MeSH
- norleucin * MeSH
Ligands containing bulky aliphatic P1 residues exhibit a high affinity towards cytosolic leucine aminopeptidase, a bizinc protease of biomedical significance. According to this specificity, a series of phosphonic and phosphinic compounds have been put forward as novel putative inhibitors of the enzyme. These phosphonic and phosphinic compounds were derivatives of methionine and norleucine as both single amino acids and dipeptides. The designed inhibitors were synthesised and tested towards the peptidase isolated from porcine kidneys using an improved separation procedure affording superior homogeneity. Unexpectedly, organophosphorus derivatives of methionine and norleucine exhibited moderate activity with K(i) values in the micromolar range.
Citace poskytuje Crossref.org
