Incorporation of neutral C-terminal residues in 3-amidinophenylalanine-derived matriptase inhibitors.
Bioorg Med Chem Lett
; 19(7): 1960-5, 2009 Apr 01.
Article
in En
| MEDLINE
| ID: mdl-19250826
ABSTRACT
A novel series of matriptase inhibitors based on previously identified tribasic 3-amidinophenylalanine derivatives was prepared. The C-terminal basic group was replaced by neutral residues to reduce the hydrophilicity of the inhibitors. The most potent compound 22 inhibits matriptase with a K(i) value of 0.43 nM, but lacks selectivity towards factor Xa. By combination with neutral N-terminal sulfonyl residues several potent thrombin inhibitors were identified, which had reduced matriptase affinity.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Phenylalanine
/
Sulfonamides
/
Serine Endopeptidases
/
Serine Proteinase Inhibitors
/
Amidines
Type of study:
Prognostic_studies
Limits:
Animals
Language:
En
Journal:
Bioorg Med Chem Lett
Journal subject:
BIOQUIMICA
/
QUIMICA
Year:
2009
Document type:
Article
Affiliation country:
Germany