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Synthesis of the proteinase inhibitor LEKTI domain 6 by the fragment condensation method and regioselective disulfide bond formation
Author(s) -
Vasileiou Zoe,
Barlos Kostas K.,
Gatos Dimitrios,
Adermann Knut,
Deraison Celine,
Barlos Kleomenis
Publication year - 2010
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.21376
Subject(s) - chemistry , fragment (logic) , regioselectivity , kallikrein , stereochemistry , disulfide bond , combinatorial chemistry , condensation , biochemistry , enzyme , physics , computer science , thermodynamics , programming language , catalysis
Proteinase inhibitors are of high pharmaceutical interest and are drug candidates for a variety of indications. Specific kallikrein inhibitors are important for their antitumor activity and their potential application to the treatment of skin diseases. In this study we describe the synthesis of domain 6 of the kallikrein inhibitor Lympho‐Epithilial Kazal‐Type Inhibitor (LEKTI) by the fragment condensation method and site‐directed cystine bridge formation. To obtain the linear LEKTI precursor, the condensation was best performed in solution, coupling the protected fragment 1‐22 to 23‐68. This method yielded LEKTI domain 6 of high purity and equipotent to the recombinantly produced peptide. © 2010 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 94: 339–349, 2010. This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com