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InterMune Presents Research on ITMN-191 in Hepatitis C at Digestive,Disease Week Meeting

Reports 'Picomolar' Potency and Slow Dissociation from HCV Protease

WASHINGTON, May 21, 2007 /PRNewswire-FirstCall via COMTEX News Network/ -- InterMune, Inc. (Nasdaq: ITMN) today presented new preclinical data on the company's Hepatitis C virus (HCV) NS3/4A protease inhibitor, ITMN-191, during a scientific session of the Digestive Disease Week (DDW) meeting being held May 19-24 in Washington, D.C. The reported study (DDW abstract #M1816) examined ITMN-191 potency and binding kinetics in biochemical assays.

The new InterMune study represents an in-depth characterization of the mechanism of inhibition of the HCV NS3/4A serine protease by ITMN-191. Full characterization of the inhibition mechanism indicated that ITMN-191's true biochemical potency of 36 picomolar (pM) was approximately ten-fold better than previously inferred (~ 250 pM reported at DDW 2006). The presented data also suggest that ITMN-191 binds to the NS3/4A protease target in a two-step binding mechanism in which ITMN-191 initially associates with NS3/4A in a collision complex that isomerizes to a long-lived but non-covalent drug-target complex. The half life of the complex between ITMN-191 and NS3/4A was estimated to be five hours or more, and inhibition of protease activity of NS3/4A was stable over this same time period. Slow dissociation of ITMN-191 from the NS3/4A protease may have a relevant in vivo consequence, as a two-hour exposure of ITMN-191 to tissue culture cells that harbor an HCV replicon resulted in an antiviral effect equal to that delivered by continuous exposure of ITMN-191.

Lawrence M. Blatt, Ph.D., Chief Scientific Officer of InterMune, said, "This preclinical study of ITMN-191 provides a better understanding of its attractive potency and binding characteristics. While ITMN-191 is a non-covalent, reversible inhibitor of the protease, the onset of inhibition and slow dissociation compare favorably with those
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