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In an attempt to develop effective inhibitors of Candida secreted aspartic proteinases, we have prepared a series of N-protected peptides varying in the type of scissile bond replacement, in the P and P' side chains as well as in the N- and C-terminal modifications. The compounds were tested in vitro with the chromogenic peptide substrate using purified secreted proteinases of C. albicans and C. tropicalis. Our results have confirmed that the binding of inhibitors and their effectiveness is influenced by a number of enzyme-inhibitor interactions. Moreover, factors like solvation/desolvation contribute to the optimal binding energy of the inhibitors.