Chemical synthesis of an octadecapeptide with the biological and immunological properties of human heat-stable Escherichia coli enterotoxin.
An eighteen-amino-acid peptide having the linear amino acid sequence of human heat-stable enterotoxin (ST) has been synthesized by solid phase peptide synthesis. The purified peptide could be obtained in yields approaching 25% after purification by size, charge, and high-performance ligand chromatography. This material was pure and identical to native ST by analytical high-performance ligand chromatography, amino acid analysis, paper electrophoresis and thin-layer chromatography. The formation of the disulfide bonds was critical for biological and immunological activity and were tentatively determined to be between cysteines 5 and 14, 6 and 10, and 9 and 17. This synthetic peptide had full immunological and biological activity when compared to native ST by enzyme-linked immunosorbent assay and the suckling mouse assay respectively.
D000595:Amino Acid Sequence; D000818:Animals; D000942:Antigens, Bacterial / Q000138:chemical synthesis; D001427:Bacterial Toxins / Q000138:chemical synthesis* / Q000276:immunology; D002851:Chromatography, High Pressure Liquid; D004220:Disulfides; D004768:Enterotoxins / Q000138:chemical synthesis* / Q000276:immunology; D004797:Enzyme-Linked Immunosorbent Assay; D004926:Escherichia coli / Q000378:metabolism; D029968:Escherichia coli Proteins; D051379:Mice; D010084:Oxidation-Reduction
D000942:Antigens, Bacterial; D001427:Bacterial Toxins; D004220:Disulfides; D004768:Enterotoxins; D029968:Escherichia coli Proteins; C034151:heat stable toxin (E coli)