Journal Article

Design, synthesis and analysis of novel bicyclic and bifunctional protease inhibitors

Agnès M. Jaulent and Robin J. Leatherbarrow

in Protein Engineering, Design and Selection

Volume 17, issue 9, pages 681-687
Published in print September 2004 | ISSN: 1741-0126
Published online September 2004 | e-ISSN: 1741-0134 | DOI: http://dx.doi.org/10.1093/protein/gzh077
Design, synthesis and analysis of novel bicyclic and bifunctional protease inhibitors

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Two novel synthetic inhibitors were designed to combine the advantageous properties of Bowman Birk inhibitor (BBI) and sunflower trypsin inhibitor-1 (SFTI-1). As is the case for BBI, the novel inhibitors have two active sites that give dual independent protease inhibition. However, they also possess a small bicyclic structure, reminiscent of the single-site SFTI-1. It is found that the synthetic inhibitors retain the potent inhibitory properties of the parent structures; they are also found to be relatively resistant to proteolysis. Their inhibition properties and a comparison of their stability to proteolysis relative to SFTI-1 are described. It is found that the new inhibitors do indeed allow bifunctional inhibition, although, unlike BBI, the small size of the inhibitor prevents the simultaneous inhibition of two proteases at the same time.

Keywords: Bowman Birk inhibitor; peptide synthesis; protease inhibitor; sunflower trypsin inhibitor

Journal Article.  5779 words.  Illustrated.

Subjects: Proteins

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