Premium
Hybrid analogues of SFTI‐1 modified in P 1 position by β‐ and γ‐amino acids and N ‐substituted β‐alanines
Author(s) -
Debowski D.,
Łukajtis R.,
Filipowicz M.,
Strzelecka P.,
Wysocka M.,
Łęgowska A.,
Lesner A.,
Rolka K.
Publication year - 2013
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.22184
Subject(s) - chemistry , peptidomimetic , amine gas treating , amino acid , stereochemistry , chymotrypsin , trypsin , alanine , peptoid , acryloyl chloride , biochemistry , enzyme , organic chemistry , peptide , monomer , acrylate , polymer
A series of compounds containing either non‐proteinogenic β‐/γ‐amino acids or N ‐substituted β‐alanine residues (β‐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 β‐alanines (βNhlys and βNhphe) 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 α‐chymotrypsin or bovine β‐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. © 2012 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 100: 154–159, 2013.