Interaction of .alpha.-dansylated peptide inhibitors with porcine pepsin: detection of complex formation by fluorescence energy transfer and chromatography and evidence for a two-step binding scheme

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Abstract
Peptide inhibitors, specifically labeled at the .alpha.-amino terminus by dansylation, were prepared by utilizing solid-phase peptide synthesis. Changes in fluorescence were observed upon mixing these peptides with porcine pepsin that can be attributed to the formation of at least 2 complexes. Energy transfer between tryptophan residues of the protein and the dansyl group of the inhibitors was detected by the unique excitation spectra generated. The kinetics of formation of the second complex can be correlated with inhibition of the catalytic activity of pepsin. Evidence for complex formation was also obtained from gel filtration experiments using the fluorescent peptides.

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