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  • Title: Design, synthesis and analysis of novel bicyclic and bifunctional protease inhibitors.
    Author: Jaulent AM, Leatherbarrow RJ.
    Journal: Protein Eng Des Sel; 2004 Sep; 17(9):681-7. PubMed ID: 15486024.
    Abstract:
    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.
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