The design, synthesis, and structure-activity relationships analysis of some potential protease inhibitors are outlined in this thesis. In particular, the serine protease thrombin and the malarial aspartic proteases plasmepsin I and II (Plm I and II) are described in regard to the roles they play in living organisms, and that is followed by discussions concerning the design, synthesis, and biological test results of inhibitors of these enzymes.

A topic considered is why it is sometimes necessary to pharmacologically regulate the blood-coagulating capacity of thrombin. Moreover, various aspects of malaria arediscussed, including the geographical distribution of the disease, the biological features of the malaria parasites, and the consequences of malaria infection.

The problems associated with designing enzyme inhibitors in general are briefly explained. Furthermore, the design of inhibitors of thrombin and Pim I and II is considered in greater detail, and the task of designing the novel potential inhibitors reported in the papers underlying this thesis is addressed.

The synthesis of thrombin inhibitors based on tartaric acid and malic acid, and the synthesis of newly designed plasmepsin inhibitors based on a novel reversed-statine core are described in detail. The utilization of solid support chemistry in the work on plasmepsin inhibitors is explained thoroughly. Additionally, there are discussions extensively covering the challenges encountered regarding the syntesis of all types of inhibitors in this thesis, and alternative synthetic strategies are addressed. Biological test results of the synthesized target compounds are analyzed, and structure-activity relationships (SAR) discussions are conducted as thoroughly as possible.