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Labeling and Protecting N ‐Terminal Protein Positions by β ‐Peptidyl Aminopeptidase‐Catalyzed Attachment of β ‐Amino‐Acid Residues – Insulin as a First Example
Author(s) -
Kolesinska Beata,
Wasko Joanna,
Kaminski Zbigniew,
Geueke Birgit,
Kohler HansPeter E.,
Seebach Dieter
Publication year - 2018
Publication title -
helvetica chimica acta
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.74
H-Index - 82
eISSN - 1522-2675
pISSN - 0018-019X
DOI - 10.1002/hlca.201700259
Subject(s) - chemistry , aminopeptidase , amino acid , amino acid residue , catalysis , peptide , biochemistry , terminal (telecommunication) , stereochemistry , combinatorial chemistry , peptide sequence , leucine , gene , telecommunications , computer science
We have shown for the first time that a natural protein (human insulin) can be acylated at the N ‐terminus with a β ‐amino acid (H‐ β 3 hAla‐), in a process catalyzed by the β ‐peptidyl aminopeptidase 3‐2W4‐BapA. This selective modification, which could also be applied for protein labeling and tagging, should be generally useful, also to protect peptides and proteins from attack by common aminopeptidases.