Abstract
During viral replication, the HIV–protease is responsible for post-translational processing of Gag and Gag-Pol polyprotein precursors [14]. The inhibition of this enzyme leads to the generation of immature non-infectious viruses and thereby to a reduction of viral spread [13]. Thus, protease inhibitors are currently the most promising drugs for the HIV therapy, especially in combination with inhibitors of the reverse transcriptase [8,10,13]. However, the protease inhibitors used so far, e. g. in the highly active anti-retroviral therapy (HAART), showed a limited capability to penetrate the cellular plasma membrane. Moreover, they exhibit a high affinity for plasma proteins resulting in a reduced in vivo efficacy, a high dose requirement [7] and toxicity. Most of these pseudo-peptides are active site inhibitors and selective for the HIV-1 protease. However, the application in therapy frequently leads to a rapid development of viral resistance [10]. These disadvantages may be overcome by inhibitors targeting alternative sites of the HIV-i protease.
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Petry, H. et al. (2000). Inhibition of HIV-1 Replication by Peptidic Protease Inhibitors. In: Brockmeyer, N.H., Hoffmann, K., Reimann, G., Stücker, M., Altmeyer, P., Brodt, R. (eds) HIV-Infekt. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-59683-4_11
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DOI: https://doi.org/10.1007/978-3-642-59683-4_11
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