Chemical synthesis of γ-echistatin analogues: elucidation of status of C-terminal (45–49)

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Abstract
Three analogues of γ-echistatin, des(45–49)-γ-echistatin, des(46–49)-y-echistatin and des(47–49)-γ-echistatin, were synthesized by solid-phase methodology and their biological activities were measured and compared. The results reveal that without the C-terminal (45–49) of γ-echistatin, the folding of the protein to the final active structure is not interfered with and Lys-45 influences the inhibition of platelet aggregation.

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