Open AccessChemical synthesis of an octadecapeptide with the biological and immunological properties of human heat‐stable Escherichia coli enterotoxin
Author(s) -
HOUGHTEN Richard A.,
OSTRESH John M.,
KLIPSTEIN Frederick A.
Publication year - 1984
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1984.tb08535.x
Subject(s) - peptide , enterotoxin , escherichia coli , amino acid , heat stable enterotoxin , peptide sequence , chromatography , chemistry , affinity chromatography , ligand (biochemistry) , biochemistry , biological activity , gel electrophoresis , disulfide bond , peptide synthesis , enzyme , receptor , in vitro , gene
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.