Aspartyl Proteinase Inhibitors

The synthetic peptide aspartyl proteinase inhibitors  are among the most intensively designed molecules. The principal recent reason for this is that HIV proteinase inhibitors turned out to be successful drugs for fighting AIDS. In contrast, the protein inhibitors of aspartyl proteinases are very little studied. It is difficult to believe that this neglect is a result of the rare occurrence of such inhibitors in nature. The activation of zymogens of aspartyl proteinases (pepsinogen) has been a problem of long-standing interest. The propeptide is clearly a pepsin inhibitor. Much more potent and typical is the pepsin inhibitor from the roundworm (Ascaris lumbricoides). The determination of the three-dimensional structure of its complex with pepsin is now in progress and may awaken this long-dormant field. A large number of reports deal with cathepsin D inhibitors classified as members of the soybean trypsin inhibitor (Kunitz), or STI family. Many of the cathepsin D inhibitors are also said to inhibit trypsin, but the details of their interaction either with cathepsin D or with trypsin have been little studied.

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