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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

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.[1]

References

  1. Solid phase synthesis of a trypsin inhibitor isolated from the Cucurbitaceae Ecballium elaterium. Le-Nguyen, D., Nalis, D., Castro, B. Int. J. Pept. Protein Res. (1989) [Pubmed]
 
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