Solid phase synthesis of a trypsin inhibitor isolated from the Cucurbitaceae Ecballium elaterium.
The synthesis of a 28-residue peptide isolated from Ecballium elaterium of the Cucurbitaceae family which strongly inhibits trypsin activities (Ka = 8.10(-11)M), using BOP as the coupling reagent in a solid phase procedure is presented. This micro protein contains three disulfide bridges in its sequence and was obtained after oxidation of the six half-cystine residues either by air or with the use of carboethoxysulfenyl chloride. After purification by semi-preparative HPLC, the synthetic product was shown by trypsin inhibition tests to be identical with the trypsin inhibitor EETI II isolated from Ecballium elaterium.
Le-Nguyen
D
D
Centre CNRS-INSERM of Pharmacology and Endocrinology, Montpellier, France.
Nalis
D
D
Castro
B
B
D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D004220:Disulfides / Q000032:analysis; D008969:Molecular Sequence Data; D010940:Plant Proteins; D010944:Plants / Q000032:analysis; D014361:Trypsin Inhibitors / Q000138:chemical synthesis* / Q000302:isolation & purification
D004220:Disulfides; D010940:Plant Proteins; D014361:Trypsin Inhibitors; C063950:trypsin inhibitor EETI II protein, plant