Semisynthesis of Arg15, Glu15, Met15, and Nle15-aprotinin involving enzymatic peptide bond resynthesis
| Autor: | Armin Mehlich, Werner Schröder, Herbert R. Wenzel, Jürgen Beckmann, Harald Tschesche |
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| Rok vydání: | 1989 |
| Předmět: |
Stereochemistry
Norleucine Glutamic Acid Arginine Biochemistry chemistry.chemical_compound Aprotinin Methionine Glutamates medicine Animals Chymotrypsin Humans Organic chemistry Peptide bond Trypsin Amino Acid Sequence Chromatography High Pressure Liquid Carbodiimide Aminocaproates chemistry.chemical_classification biology Hydrolysis Semisynthesis Peptide Fragments Amino acid chemistry biology.protein Electrophoresis Polyacrylamide Gel medicine.drug |
| Zdroj: | Journal of Protein Chemistry. 8:101-113 |
| ISSN: | 1573-4943 0277-8033 |
| DOI: | 10.1007/bf01025082 |
| Popis: | The semisynthesis of homologues of aprotinin, the bovine pancreatic trypsin inhibitor, is described. The P1 lysine15 residue was replaced by two methods. The first procedure, which consisted of two enzymatic steps for the incorporation of other amino acids has previously been described. The second approach consisted of six steps of both enzymatic and chemical nature. The modified inhibitor, in which the lysine15-alanine16 peptide bond is hydrolyzed, was used as the starting material. All carboxyl groups of the modified inhibitor were esterified with methanol; the lysine15 methylester group was then selectively hydrolyzed. Afterward, lysine15 itself was split off. Arginine, glutamic acid, methionine, and L-2-aminohexanoic acid (norleucine, Nle) were incorporated using water-soluble carbodiimide combined with an acylation catalyst. The methylester group was used to prevent polymerization. The reactive-site peptide bonds were resynthesized using either chymotrypsin or trypsin. |
| Databáze: | OpenAIRE |
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