Work

Inhibition of pepsin by analogues of pepsinogen-(1–12)-peptide with substitutions in the 4–7 sequence region

Year: 1983

Type: article

Abstract: Derivatives of the 1-12 sequence of pig pepsinogen were prepared by solid-phase peptide synthesis. The three derivatives contain substitutions in the 4-7 region of the 1-12 sequence. Glycine was used to replace the hydrophobic residues -Val-Pro-Leu-Val- in pairs. After cleavage and purification, the synthetic peptides were compared with a synthetic peptide of the native sequence, prepared at the same time, with respect to their ability to inhibit the pepsin-catalysed clotting of milk. Inhibitory potency, determined from plots of percentage inhibition versus concentration of synthetic peptide, is inversely correlated with the substitution of glycine residues for the hydrophobic residues. Therefore the equilibrium inhibition of pepsin by these peptides is dominated by the hydrophobic nature of the 4-7 sequence region.

Source: Biochemical Journal

DOI: 10.1042/bj2090355

Authors: B M Dunn, M Lewitt, C Pham

Institution: University of Florida

Language: English

Topic: Protease and Inhibitor Mechanisms

Subfield: Cancer Research

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: bronze

Funder: National Institutes of Health

Award: MECHANISM OF PEPSIN CATALYSIS AND INHIBITION