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Fluorescent analogs of trypsin inhibitor SFTI-1 isolated from sunflower seeds—synthesis and applications
Article first published online: 17 JAN 2014
Copyright © 2013 Wiley Periodicals, Inc.
Volume 102, Issue 1, pages 124–135, January 2014
How to Cite
Lesner, A., Karna, N., Psurski, M., Łęgowska, A., Wysocka, M., Guzow, K., Sieradzan, A., Sieńczyk, M., Trzonkowski, P., Pikuła, M., Zieliński, M., Kosikowska, P., Łukajtis, R., Łęgowska, M., Dębowski, D., Wiczk, W. and Rolka, K. (2014), Fluorescent analogs of trypsin inhibitor SFTI-1 isolated from sunflower seeds—synthesis and applications. Biopolymers, 102: 124–135. doi: 10.1002/bip.22442
- Issue published online: 17 JAN 2014
- Article first published online: 17 JAN 2014
- Accepted manuscript online: 25 NOV 2013 01:36AM EST
- Manuscript Accepted: 7 NOV 2013
- Manuscript Revised: 15 OCT 2013
- Manuscript Received: 18 JUL 2013
- National Science Centre (NCN)
- proteinase inhibitors;
This article describes the synthesis and enzymatic study of newly synthesized analogs of trypsin inhibitors SFTI-1 that were fluorescent labeled on their N-terminal amino groups. Two fluorescent derivatives of benzoxazole (3-[2-(4-diphenylaminophenyl)benzoxazol-5-yl]-l-alanine–[(4NPh2)Ph]Box-Ala and 3-[2-(2',4',5'-trimethoxyphenyl)benzoxazol-5-yl]-l-alanine–[2,4,5-(OMe)3Ph]Box-Ala) were used as efficient fluorescent labels. The compounds obtained preserved their inhibitory activity and were efficient inhibitors of bovine trypsin or chymotrypsin. Nevertheless, their association inhibition constants were one or two orders of magnitude lower than those determined for unlabeled monocyclic SFTI-1 or [Phe5]SFTI-1, respectively. The conjugates obtained were found to be proteolytically stable in the presence of cognate enzymes. Applying such fluorescent peptides, we were able to investigate enzyme-inhibitor complex formation using fluorescent techniques. We found that such compounds were rapidly internalized by the fibroblast or cancer cells with no cytotoxic effects. © 2013 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 102: 124–135, 2014.