Thermodynamics of formation of the insulin hexamer: metal-stabilized proton-coupled assembly of quaternary structure

Biochemistry. 2014 Mar 4;53(8):1296-301. doi: 10.1021/bi4016567. Epub 2014 Feb 18.

Abstract

The thermodynamics of formation of the insulin hexamer, which is stabilized by two Zn(2+) ions, were quantified by isothermal titration calorimetry (ITC). Because the insulin monomer is unstable to aggregation (fibrillation) during ITC measurements, an original method involving EDTA chelation of Zn(2+) from the hexamer was employed. The two metal ions are chelated sequentially, reflecting stepwise Zn(2+) binding and stabilization of the quaternary structure. Analysis of the ITC data reveals that two to three H(+) bind to the hexamer upon its formation at pH 7.4, which is both enthalpically and entropically favored. The former is due to Zn(2+) coordination to His residues from three subunits, and the latter is associated with desolvation that accompanies the protonation and the packing of the subunits in the hexamer.

Publication types

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

MeSH terms

  • Humans
  • Insulin / chemistry*
  • Insulin / metabolism
  • Models, Molecular
  • Protein Multimerization* / drug effects
  • Protein Stability / drug effects
  • Protein Structure, Quaternary / drug effects
  • Protons*
  • Thermodynamics
  • Zinc / metabolism*
  • Zinc / pharmacology

Substances

  • Insulin
  • Protons
  • Zinc