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Peptide splicing in a double‐sequence analogue of trypsin inhibitor SFTI‐1 substituted in the P 1 positions by peptoid monomers
Author(s) -
Kartalia,
Dębowski Dawid,
Łęgowska Anna,
Bąchor Remigiusz,
Szewczuk Zbigniew,
Rolka Krzysztof
Publication year - 2015
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.22659
Subject(s) - peptoid , chemistry , trypsin , peptide , monomer , sequence (biology) , trypsin inhibitor , stereochemistry , biochemistry , enzyme , organic chemistry , polymer
Recently, we described a process of trypsin‐assisted peptide splicing of analogs of trypsin inhibitor SFTI‐1, that seems to be very similar to proteasome‐catalyzed peptide splicing. Here, we show, for the first time, that a peptide–peptoid hybrid (peptomer) can also be spliced by trypsin. Incubation of a double sequence SFTI‐1 analog, containing two peptoid monomers, with equimolar amount of trypsin leads to formation of monocyclic peptomer as the main product. We proved that the peptide bond formed by a peptoid monomer is not only digested by trypsin but also participates in the enzyme‐assisted splicing process. © 2015 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 104: 206–212, 2015.