A series of compounds containing either non-proteinogenic beta-/gamma-amino acids or N-substituted beta-alanine residues (beta-peptoid units) in P-1 specificity position were synthesized based on the structure of sunflower trypsin inhibitor 1 (SFTI-1). The compounds were synthesized on a solid support; the N-substituted beta-alanines (beta Nhlys and beta Nhphe) were introduced into a peptidomimetic chain via a two-step approach using acryloyl chloride and an appropriate primary amine. The inhibitory activities were characterized in vitro against bovine alpha-chymotrypsin or bovine beta-trypsin. Three analogues displayed activity comparable to fully proteinogenic counterparts-monocyclic SFTI-1 and [Phe(5)] SFTI-1. Moreover, all active peptidomimetics were resistant toward proteolytic degradation, even after 24-h incubation at room temperature. (C) 2012 Wiley Periodicals, Inc
Authors
- D. Debowski,
- R. Łukajtis,
- M. Filipowicz,
- P. Strzelecka,
- M. Wysocka,
- A. Łęgowska,
- A. Lesner,
- K. Rolka,
- Rafał Łukajtis link open in new tab ,
- Adam Lesner link open in new tab
Additional information
- DOI
- Digital Object Identifier link open in new tab 10.1002/bip.22184
- Category
- Publikacja w czasopiśmie
- Type
- artykuł w czasopiśmie wyróżnionym w JCR
- Language
- angielski
- Publication year
- 2013
