Solid-phase synthesis of a peptide-ligand affinity matrix for isolation of chymosin

Pept Res. 1993 Nov-Dec;6(6):320-9.

Abstract

Aminopropyl Perloza beaded cellulose was used as the support for solid-phase synthesis of resin-bound Val-dLeu-Pro-Phe-Phe-Val-dLeu, an inhibitor of aspartic proteases. Both Boc and Fmoc SPPS methodologies were employed in separate syntheses. The peptide-resins were characterized by amino acid analysis. The peptide-resin from the Fmoc synthesis gave the better amino acid analysis of the two syntheses and was used for further studies. Following modification of the peptide N-terminus by succinylation, the peptide-resin was able to bind chymosin (E.C. 3.5.21.4). The peptide resin was used for isolation of chymosin from a crude recombinant broth.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amino Acids
  • Aspartic Acid Endopeptidases / antagonists & inhibitors
  • Cellulose
  • Chromatography, Affinity*
  • Chymosin / isolation & purification*
  • Chymosin / metabolism
  • Fluorenes
  • Formic Acid Esters
  • Ligands
  • Molecular Sequence Data
  • Oligopeptides / chemical synthesis*
  • Oligopeptides / metabolism
  • Protease Inhibitors / chemical synthesis*
  • Protease Inhibitors / chemistry
  • Recombinant Proteins / isolation & purification
  • Resins, Plant

Substances

  • Amino Acids
  • Fluorenes
  • Formic Acid Esters
  • Ligands
  • N(alpha)-fluorenylmethyloxycarbonylamino acids
  • Oligopeptides
  • Protease Inhibitors
  • Recombinant Proteins
  • Resins, Plant
  • t-butyloxycarbonyl group
  • succinyl-valyl-leucyl-prolyl-phenylalanyl-phenylalanyl-valyl-leucinamide
  • Cellulose
  • Aspartic Acid Endopeptidases
  • Chymosin