Urea-diketopiperazine interactions: a model for urea induced denaturation of proteins

Biophys Chem. 1993 Apr;46(2):171-7. doi: 10.1016/0301-4622(93)85024-c.

Abstract

The solubility of diketopiperazine (DKP) in aqueous urea (U) solutions with molalities ranging from 0 to 16 mol kg-1 (corresponding to urea activities ranging from 0 to 10 mol kg-1) has been measured as a function of the urea activity at 298.15 K. In accordance with a previous study the solubility of diketopiperazine increases with increasing urea activity but drops sharply at a urea activity of 5.7 +/- 0.2 mol kg-1. This drop in solubility can be attributed to the formation of a DKP.U2 cocrystal. The solubility data were fitted to a simple model based on the stoichiometry of the DKP.U2 to yield an intrinsic equilibrium constant kappa describing the interactions occurring between a urea molecule and a peptide group of diketopiperazine in aqueous solution, its value being kappa = 0.0447 +/- 0.0007 kg mol-1. When the activity of water is taken into account, kappa has a lower value of 0.0398 +/- 0.0007 kg mol-1.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Crystallization
  • Diketopiperazines
  • Dipeptides / chemistry
  • Models, Chemical
  • Piperazines / chemistry*
  • Protein Denaturation
  • Urea / chemistry*

Substances

  • Diketopiperazines
  • Dipeptides
  • Piperazines
  • Urea