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Investigation of peptide splicing using two‐peptide‐chain analogs of trypsin inhibitor SFTI ‐1
Author(s) -
Kartalia,
Dębowski Dawid,
Gitlin Agata,
Łęgowska Anna,
Rolka Krzysztof
Publication year - 2013
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.12542
Subject(s) - peptide , trypsin , chemistry , peptide bond , serine , proteolysis , serine protease , biochemistry , proteasome , chymotrypsin , rna splicing , stereochemistry , protease , enzyme , gene , rna
This study examines peptide splicing catalyzed by serine proteinases. A series of two‐peptide‐chain analogs of trypsin inhibitor SFTI ‐1 were designed and synthesized via the solid‐phase method. All consisted of two peptide chains (also called N‐ and C‐terminal fragments) joined together by one disulfide bridge. The analogs were incubated with bovine β‐trypsin or bovine α‐chymotrypsin. Analysis of MS data analysis showed that, after enzyme‐catalyzed degradation of the single peptide bond between the Lys and Ser residues located at the C‐terminus of the C‐terminal peptide chain, a new peptide bond was formed. This bond brought together the separated peptide chains, and, as a result, monocyclic SFTI ‐1 was recovered. This proteolytic route of peptide rearrangement appears to be similar to peptide splicing catalyzed by proteasomes. However, the proteasome is much more complex than ‘classical’ serine proteinases.