Czasopismo
1998
|
[Z] 52, 11-12
|
871--887
Tytuł artykułu
Autorzy
Wybrane pełne teksty z tego czasopisma
Warianty tytułu
Low molecular inhibitors of plasmin
Języki publikacji
Abstrakty
Plasmin, serine protease with trypsin specifity, plays a key role in the process of fibrinolysis. Analogs of lysine like e-aminocaproic acid and trans-4-aminomethylclohexanecarboxylic acid are employed clinically as plasmin inhibitors and exhibit an inhibitory effect by blocking lysine binding sites of the enzyme. Their inhibitory activity on plasmin with the respect to fibrinogen and other proteins is much weaker than towards fibrin. Because of this reason investigations on the synthesis of an active centre directed inhibitors of plasmin were also undertaken. A great number of compounds was obtained including derivatives of w-aminoacids or lysine. Next important group were short peptides with C-terminal lysine or arginine derivatives such as aldehydes, chloromethylketones, fluoromethylketone, methylketones, amides or esters. This paper presents literature data on structure-activity relationship for low molecular inhibitors of plasmin with a structure of aminoacids or peptides derivatives.
Słowa kluczowe
Czasopismo
Rocznik
Tom
Strony
871--887
Opis fizyczny
Bibliogr. 52 poz., rys., schem.
Twórcy
autor
- Instytut Chemii, Uniwersytet w Białymstoku, ul. J. Piłsudskiego 11/4, 15-443 Białystok
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Uwagi
PL
Typ dokumentu
Bibliografia
Identyfikatory
Identyfikator YADDA
bwmeta1.element.baztech-article-BUS1-0002-0092