The role of some polar amino acid residues in secretin

Abstract

Three analogues of S5-27, the tricosapeptide with the carboxyl-terminal sequence of secretin, were studied. In the analogues, the acidic residues at positions 9 and 15 of S5-27 were replaced by the neutral residues glutamine and asparagine. These changes resulted in a decrease in immunoreactivity. Binding to an antibody against secretin could be correlated with the changes in the conformation of the synthetic analogues.