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Analogues of trypsin inhibitor SFTI-1 modified in the conserved P1′ position by synthetic or non-proteinogenic amino acids retain their inhibitory activity
Abstrakt
A series of linear and monocyclic (with a disulfide bridge only) analogues of trypsin inhibitor SFTI-1 modified in the P-1 and/or P-1' positions were synthesized by the solid-phase method. In the substrate specificity P-1 position, Phe or N-benzylglycine (Nphe) were introduced, whereas the conserved Ser6 in Bownam-Birk (BBI) inhibitors was replaced by Hse (L-homoserine), Nhse [N-(2-hydroxyethyl)glycine], Sar, and Ala. Kinetic studies of interaction of the analogues with bovine alpha-chymotrypsin have shown that in monocyclic (but not linear) analogues, Hse and Nhse are tolerated to afford potent inhibitors. This is the first evidence that the absolutely conserved Ser present in the inhibitor's P-1' position can be successfully replaced by a synthetic derivative. Copyright (C) 2011 European Peptide Society and John Wiley & Sons, Ltd.
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Autorzy (7)
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Łukajtis Rafał
- University of Gdansk
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Łȩgowska Anna
- University of Gdansk
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Wysocka Magdalena
- University of Gdansk
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Dȩbowski Dawid
- University of Gdansk
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Lesner Adam
- University of Gdansk
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Rolka Krzysztof
- University of Gdansk
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Informacje szczegółowe
- Kategoria:
- Publikacja w czasopiśmie
- Typ:
- artykuł w czasopiśmie wyróżnionym w JCR
- Opublikowano w:
-
JOURNAL OF PEPTIDE SCIENCE
nr 17,
wydanie 4,
strony 281 - 287,
ISSN: 1075-2617 - Język:
- angielski
- Rok wydania:
- 2011
- Opis bibliograficzny:
- Rafał Ł., Anna Ł., Magdalena W., Dawid D., Adam L., Krzysztof R.: Analogues of trypsin inhibitor SFTI-1 modified in the conserved P1′ position by synthetic or non-proteinogenic amino acids retain their inhibitory activity// JOURNAL OF PEPTIDE SCIENCE. -Vol. 17, iss. 4 (2011), s.281-287
- DOI:
- Cyfrowy identyfikator dokumentu elektronicznego (otwiera się w nowej karcie) 10.1002/psc.1330
- Weryfikacja:
- Politechnika Gdańska
wyświetlono 68 razy
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