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Chemical Compound Review:

Mozenavir (4R,5S,6S,7R)-1,3-bis[(3...

Synonyms: DMP-450, dmp450, CHEMBL223824, SureCN3455127, CHEBI:41994, ...

Hodge, C.N. et al., Hylton, K.G. et al., Toma, E. et al., Vickery, R.D. et al.

Hodge, Aldrich, Bacheler, Chang, Eyermann, Garber, Grubb, Jackson, Jadhav, Korant, Lam, Maurin, Meek, Otto, Rayner, Reid, Sharpe, Shum, Winslow, Erickson-Viitanen,

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Disease relevance of dmp450

DMP 450 is highly selective for HIV protease, consistent with displacement of the retrovirus-specific structural water molecule [1].
Improved cyclic urea inhibitors of the HIV-1 protease: synthesis, potency, resistance profile, human pharmacokinetics and X-ray crystal structure of DMP 450 [1].

High impact information on dmp450

RALDH activity was heightened by ritonavir (24%), indinavir (17%), saquinavir (17%), zalcitabine (14%), delavirdine (12%) and nelfinavir (10%) and decreased (22%) by DMP-450 [2].
CONCLUSIONS: DMP 450 is a significant advance within the cyclic urea class of HIV protease inhibitors due to its exceptional oral bioavailability [1].
RESULTS: We have synthesized DMP 450 (bis-methanesulfonic acid salt), a water-soluble cyclic urea compound and a potent inhibitor of HIV replication in cell culture that also inhibits variants of HIV with single amino acid substitutions in the protease [1].
As an illustration, the core structure of the HIV protease inhibitors DMP 323 and DMP 450 has been prepared by catalytic carbonylation of diamine intermediates from the original syntheses [3].
The degradation of the HIV protease inhibitor, DMP 450, in a binary mixture with hydrous lactose was followed in the presence of 5% additional water [4].

References

Improved cyclic urea inhibitors of the HIV-1 protease: synthesis, potency, resistance profile, human pharmacokinetics and X-ray crystal structure of DMP 450. Hodge, C.N., Aldrich, P.E., Bacheler, L.T., Chang, C.H., Eyermann, C.J., Garber, S., Grubb, M., Jackson, D.A., Jadhav, P.K., Korant, B., Lam, P.Y., Maurin, M.B., Meek, J.L., Otto, M.J., Rayner, M.M., Reid, C., Sharpe, T.R., Shum, L., Winslow, D.L., Erickson-Viitanen, S. Chem. Biol. (1996) [Pubmed]
HIV-protease inhibitors alter retinoic acid synthesis. Toma, E., Devost, D., Chow Lan, N., Bhat, P.V. AIDS (2001) [Pubmed]
Catalytic carbonylation of functionalized diamines: application to the core structure of DMP 323 and DMP 450. Hylton, K.G., Main, A.D., McElwee-White, L. J. Org. Chem. (2003) [Pubmed]
Utility of microcalorimetry in the characterization of the browning reaction. Vickery, R.D., Maurin, M.B. Journal of pharmaceutical and biomedical analysis. (1999) [Pubmed]

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