Abstract
Several analogues of heat-stable enterotoxins (ST h and ST P) produced by enterotoxigenic Escherichia coli were synthesized. Peptides (ST h[6–18] and ST P[5–17]) consisting of 13 amino acid residues from the Cys residue near the N-terminus to the Cys residue near the C-terminus and linked by three disulfide bonds had the same biological and immunological properties as native ST h and ST P, respectively. The results indicated that the sequence with the 13 amino acid residues and three disulfide linkages is essential for full biological activity of ST.
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