Peptide splicing in a double‐sequence analogue of trypsin inhibitor SFTI‐1 substituted in the P1 positions by peptoid monomers. Issue 3 (May 2015)

• Record Type: Journal Article
• Authors: Karna, Natalia; Dębowski, Dawid; Łęgowska, Anna; Bąchor, Remigiusz; Szewczuk, Zbigniew; Rolka, Krzysztof
• Is Part Of: Biopolymers. Volume 104:Issue 3(2015)
• Page Start: 206
• Page End: 212
• Publication Date: 2015-05
• Subjects: peptide splicing -- peptomer -- SFTI‐1 inhibitor -- mass spectrometry; Biopolymers -- Periodicals; Peptides -- Periodicals; Spectrum analysis -- Periodicals; 572.33
• DOI: 10.1002/bip.22659
• Languages: English
• ISSNs: 0006-3525

Abstract

Abstract: 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.