Publication Details

Reference Category Journals
DOI / URL link
Title (Primary) Therapeutic potential of the peptide leucine arginine as a new nonplant Bowman-Birk-like serine protease inhibitor
Author Rothemund, S.; Sönnichsen, F.D.; Polte, T.;
Journal Journal of Medicinal Chemistry
Year 2013
Department IMMU;
Volume 56
Issue 17
Language englisch;
POF III (all) F11;
UFZ wide themes RU3;
Abstract

The peptide leucine arginine (pLR) belongs to a new class of cyclic peptides isolated from frog skin. Its primary sequence is similar to the reactive loop of plant Bowman–Birk inhibitors (BBI), and the recently discovered circular sunflower trypsin inhibitor-1 (SFTI-1). The conformational properties of pLR in solution were determined by NMR spectroscopy and revealed excellent structural similarity to BBI and SFTI-1. Moreover, pLR is a highly potent trypsin inhibitor, with Ki values in the nanomolar range, and, due to its small size, a potential inhibitor of the serine protease tryptase. Since tryptase plays a crucial role in the development of allergic airway inflammation, the therapeutic potential of pLR in a murine asthma model was investigated. Treatment of ovalbumin-sensitized mice with pLR during allergen challenge reduced the acute asthma phenotype. Most importantly, application even at the end of a long-lasting chronic asthma model decreased the development of chronic airway inflammation and tissue remodeling.

ID 13967
Persistent UFZ Identifier https://www.ufz.de/index.php?en=20939&ufzPublicationIdentifier=13967
Rothemund, S., Sönnichsen, F.D., Polte, T. (2013):
Therapeutic potential of the peptide leucine arginine as a new nonplant Bowman-Birk-like serine protease inhibitor
J. Med. Chem. 56 (17), 6732 - 6744