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Sequoia Pharmaceuticals Presents In Vitro and First-in-Human Data Supporting Further Development of SPI-256, a Novel Investigational Protease Inhibitor
Date:10/26/2008

WASHINGTON, Oct. 26 /PRNewswire/ -- Sequoia Pharmaceuticals presented positive results today from two studies on SPI-256, a novel investigational HIV protease inhibitor (PI). One study based on an in vitro analysis demonstrates that the mode of interaction of SPI-256 with HIV protease provides a rationale for its high potency and high genetic barrier to resistance. The second study conducted in healthy volunteers demonstrates that SPI-256 is generally safe and well tolerated in humans and is amenable to boosting by pharmacokinetic enhancers (PKEs). The data were presented at the 48th annual Interscience Conference on Antimicrobial Agents and Chemotherapy (ICAAC)/46th annual Infectious Diseases Society of America (IDSA) joint meeting held in Washington, D.C.

"Two ongoing significant needs in contemporary HIV therapy are: new agents that have activity against mutant virus and also have a high genetic barrier to developing resistance; and new agents that can boost the pharmacokinetic levels of existing drugs," said Martin Markowitz, MD, professor and clinical director at the Aaron Diamond AIDS Research Center. "These data on SPI-256 look very promising and address the need for new agents with activity against protease inhibitor-resistant virus as well as the development of resistance. I look forward to further advancements and innovations in HIV that will address our needs in the treatment community from a resistance, as well as a PK, point of view."

Data on SPI-256 at this conference

Discovery and in vitro activity of SPI-256

Scientists from Sequoia Pharmaceuticals presented their structure-based approach that led to the development of SPI-256. Prior to discovering SPI-256, Sequoia scientists examined three-dimensional structures of wild-type and drug-resistant mutant HIV proteases bound to selected inhibitors. By analyzing these structures, the Sequoia scientists were able to identify a subset of main-chain and active-site atoms of
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