Mode of disulfide bond formation of a heat-stable enterotoxin (STh) produced by a human strain of enterotoxigenic Escherichia coli |
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| Authors: | Y Shimonishi Y Hidaka M Koizumi M Hane S Aimoto T Takeda T Miwatani Y Takeda |
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| Institution: | 1. Institute for Protein Research, Osaka University, Suita, Osaka 565, Japan;2. National Children''s Medical Research Center, Setagaya-ku, Tokyo 154, Japan;3. Research Institute for Microbial Diseases, Osaka University, Suita, Osaka 565, Japan;4. The Institute of Medical Science, The University of Tokyo, Minato-ku, Tokyo 108, Japan |
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| Abstract: | To determine the modes of three disulfide linkages in the heat-stable enterotoxin (STh) produced by a human strain of enterotoxigenic Escherichia coli, we synthesized STh(6-18), which consists of 13 amino acid residues and has the same intramolecular disulfide linkages as native STh (1985) FEBS Lett. 181, 138-142], by stepwise and selective formation of disulfide bonds using different types of removable protecting groups for the Cys residues. Synthesis of the peptide with different modes of disulfide bond formation provided three peptides consistent with standard STh(6-18) in their physicochemical and biological properties, thereby indicating that the disulfide bonds in STh(6-18) are Cys-Cys-Glu-Leu-Cys-Cys-Asn-Pro-Ala-Cys-Thr-Gly-Cys. |
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