Lipase-catalyzed synthesis of precursor dipeptides of RGD in aqueous water-miscible organic solvents

Prep Biochem Biotechnol. 2003 Feb;33(1):1-12. doi: 10.1081/PB-120018365.

Abstract

PPL-catalyzed synthesis of the precursor dipeptides of RGD as a cellular adhesion factor, Benzyl-Arg-Gly-NH2 and CBZ-Gly-Asp-NH2, was conducted in water-organic cosolvents systems. Five water-miscible organic solvents, which have some advantage over the water-immiscible organic solvent systems or the anhydrous organic solvent systems used often in protease-catalyzed synthesis of a peptide bond, were tested. The reaction condition of PPL-catalyzed synthesis of the dipeptides was optimized by examining the main factors affecting the product yield. The optimal reaction condition for the synthesis of Benzyl-Arg-Gly-NH2 was set up as pH 8.0, 15 degrees C in 40% MeOH for 10 h with the maximum yield of 73.6%. The optimum condition for the synthesis of CBZ-Gly-Asp-NH2 was pH 7.0, 15 degrees C in 50% MeOH for 10h with the maximum yield of 67.0%.

Publication types

  • Evaluation Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Catalysis
  • Dipeptides / chemical synthesis*
  • Dipeptides / chemistry
  • Dipeptides / isolation & purification*
  • Enzyme Activation
  • Hydrogen-Ion Concentration
  • Lipase / chemistry*
  • Oligopeptides / chemical synthesis*
  • Oligopeptides / chemistry
  • Protein Precursors / chemical synthesis*
  • Protein Precursors / chemistry
  • Protein Precursors / isolation & purification*
  • Solvents / chemistry
  • Temperature
  • Water / chemistry

Substances

  • Dipeptides
  • Oligopeptides
  • Protein Precursors
  • Solvents
  • Water
  • arginyl-glycyl-aspartic acid
  • Lipase