Preparation of chemically 'mutated' aprotinin homologues by semisynthesis. P1 substitutions change inhibitory specificity.

Abstract

The semisynthesis of homologues of aprotinin (BPTI) is described. The P1 amino acid residue of these homologues was substituted by other amino acids using peptide synthetic methods. The reactive-site-modified inhibitor (with the Lys15-Ala16 peptide bond hydrolyzed) was used as starting material. All carboxyl groups of the modified inhibitor were esterified… (More)

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@article{Beckmann1988PreparationOC, title={Preparation of chemically 'mutated' aprotinin homologues by semisynthesis. P1 substitutions change inhibitory specificity.}, author={J. S. Beckmann and Agnieszka Mehlich and W. Schr{\"o}der and Herbert R. Wenzel and Harald Tschesche}, journal={European journal of biochemistry}, year={1988}, volume={176 3}, pages={675-82} }