Introduction of Pro and Its Analogues in the Conserved P1 Position of Trypsin Inhibitor SFTI-1 Retains Its Inhibitory Activity
Abstrakt
A number of monocyclic SFTI-1 analogues modified in the conserved inhibitor P1 position by Pro, its L-hydroxyproline (Hyp) derivative as well as mimetics with different ring size were synthesized by the solid-phase method. Replacement of Ser6 by Pro, Hyp, and a four-member ring, L-azetidine-2-carboxylic acid (Aze), retained trypsin or chymotrypsin inhibitory activity. The determined association equilibrium constants of these analogues with a cognate enzyme were about two orders of magnitude lower than those obtained for ones with conserved Ser6. In all analogues, with the exception of one, [Phe5,Aze6]SFTI-1, the P1-P1 reactive site remained intact. The results provide first evidence that the conserved Ser in the P1 position of Bowman-Birk inhibitors can be successfully replaced by an amino acid with a secondary amine group.
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- Wersja publikacji
- Accepted albo Published Version
- DOI:
- Cyfrowy identyfikator dokumentu elektronicznego (otwiera się w nowej karcie) 10.2174/092986611797201002
- Licencja
- Copyright (2011 Bentham Science Publishers)
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Informacje szczegółowe
- Kategoria:
- Publikacja w czasopiśmie
- Typ:
- artykuł w czasopiśmie wyróżnionym w JCR
- Opublikowano w:
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PROTEIN AND PEPTIDE LETTERS
nr 18,
wydanie 11,
strony 1158 - 1167,
ISSN: 0929-8665 - Język:
- angielski
- Rok wydania:
- 2011
- Opis bibliograficzny:
- Legowska A., Debowski D., Lukajtis R., Sztabkowska E., Mizeria A., Brzozowski K., Wysocka M., Lesner A., Rolka K.: Introduction of Pro and Its Analogues in the Conserved P1 Position of Trypsin Inhibitor SFTI-1 Retains Its Inhibitory Activity// PROTEIN AND PEPTIDE LETTERS. -Vol. 18, iss. 11 (2011), s.1158-1167
- DOI:
- Cyfrowy identyfikator dokumentu elektronicznego (otwiera się w nowej karcie) 10.2174/092986611797201002
- Weryfikacja:
- Politechnika Gdańska
wyświetlono 119 razy
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