Structural highlights
Publication Abstract from PubMed
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.
Therapeutic Potential of the Peptide Leucine Arginine As a New Nonplant Bowman-Birk-Like Serine Protease Inhibitor.,Rothemund S, Sonnichsen FD, Polte T J Med Chem. 2013 Aug 29. PMID:23988198[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Rothemund S, Sonnichsen FD, Polte T. Therapeutic Potential of the Peptide Leucine Arginine As a New Nonplant Bowman-Birk-Like Serine Protease Inhibitor. J Med Chem. 2013 Aug 29. PMID:23988198 doi:10.1021/jm4005362
