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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Anionic- and lipophilic-mediated surface binding inhibitors of human leukocyte elastase.

We report the synthesis of a series of diphenylmethane-based oligomers containing anionic and lipophilic functionalities that are potent inhibitors of human leukocyte elastase ( HLE). The enzyme inhibition is regulated by the size of the oligomer, as well as, the number of charges. Lipophilicity is an important element in determining potency and specificity against other basic enzymes. Compounds whose scaffolds contain three phenoxyacetic acid groups and three alkyl ethers are competitive and specific inhibitors of HLE with Ki = 20 nM. The mechanism of action of this class of compounds is believed to involve multidendate interactions with the surface of HLE near the active site which prevents substrate access to the catalytic site.[1]


  1. Anionic- and lipophilic-mediated surface binding inhibitors of human leukocyte elastase. Regan, J., McGarry, D., Bruno, J., Green, D., Newman, J., Hsu, C.Y., Kline, J., Barton, J., Travis, J., Choi, Y.M., Volz, F., Pauls, H., Harrison, R., Zilberstein, A., Ben-Sasson, S.A., Chang, M. J. Med. Chem. (1997) [Pubmed]
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