New aza-dipeptide analogues as potent and orally absorbed HIV-1 protease inhibitors: candidates for clinical development

  • J Med Chem. 1998 Aug 27;41(18):3387-401. doi: 10.1021/jm970873c.
G Bold  1 ,  A Fässler ,  H G Capraro ,  R Cozens ,  T Klimkait ,  J Lazdins ,  J Mestan ,  B Poncioni ,  J Rösel ,  D Stover ,  M Tintelnot-Blomley ,  F Acemoglu ,  W Beck ,  E Boss ,  M Eschbach ,  T Hürlimann ,  E Masso ,  S Roussel ,  K Ucci-Stoll ,  D Wyss ,  M Lang
Affiliations
  • 1. Research Laboratories Cancer and Infectious Diseases, Ciba-Geigy AG, CH-4002 Basel, Switzerland.
Abstract

On the basis of previously described X-ray studies of an enzyme/aza-dipeptide complex,8 aza-dipeptide analogues carrying N-(bis-aryl-methyl) substituents on the (hydroxethyl)hydrazine moiety have been designed and synthesized as HIV-1 Protease Inhibitors. By using either equally (12) or orthogonally (13) protected dipeptide isosteres, symmetrically and asymmetrically acylated aza-dipeptides can be synthesized. This approach led to the discovery of very potent inhibitors with Antiviral activities (ED50) in the subnanomolar range. Acylation of the (hydroxethyl)hydrazine dipeptide isostere with the L-tert-leucine derivative 29 increased the oral bioavailability significantly when compared to the corresponding L-valine or L-isoleucine derivatives. The bis(L-tert-leucine) derivatives CGP 75355, CGP 73547, CGP 75136, and CGP 75176 combine excellent Antiviral activity with high blood concentration after oral administration. Furthermore, they show no cross-resistance with saquinavir-resistant strains and maintain activity against indinavir-resistant ones. Consequently they qualify for further profiling as potential clinical candidates.

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