Search
Introduction of Pro and Its Analogues in the Conserved P1 Position of Trypsin Inhibitor SFTI-1 Retains Its Inhibitory Activity
Abstract
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.
Citations
-
4
CrossRef
-
0
Web of Science
-
4
Scopus
Authors (9)
-
Anna Legowska
-
Dawid Debowski
-
Rafal Lukajtis
-
Emilia Sztabkowska
-
Aneta Mizeria
-
Krzysztof Brzozowski dr
-
Magdalena Wysocka
-
Krzysztof Rolka
Cite as
Full text
full text is not available in portal
Keywords
Details
- Category:
- Articles
- Type:
- artykuł w czasopiśmie wyróżnionym w JCR
- Published in:
-
PROTEIN AND PEPTIDE LETTERS
no. 18,
edition 11,
pages 1158 - 1167,
ISSN: 0929-8665 - Language:
- English
- Publication year:
- 2011
- Bibliographic description:
- 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:
- Digital Object Identifier (open in new tab) 10.2174/092986611797201002
- Verified by:
- Gdańsk University of Technology
seen 76 times
Recommended for you
Analogues of trypsin inhibitor SFTI-1 modified in the conserved P1′ position by synthetic or non-proteinogenic amino acids retain their inhibitory activity
- Ł. Rafał,
- Ł. Anna,
- W. Magdalena
- + 4 authors
Functionalized Peptide Fibrils as a Scaffold for Active Substances in Wound Healing
- J. Sawicka,
- E. Iłowska,
- M. Deptuła
- + 10 authors
Fluorescent analogs of trypsin inhibitor SFTI-1 isolated from sunflower seeds-synthesis and applications
- A. Lesner,
- N. Karna,
- M. Psurski
- + 14 authors