Synthesis of lysozyme-metallacarborane conjugates and the effect of boron cluster modification on protein structure and function

Chembiochem. 2015 Feb 9;16(3):424-31. doi: 10.1002/cbic.201402611. Epub 2015 Jan 14.

Abstract

Two complementary methods, "in solution" and "in solid state", for the synthesis of lysozyme modified with metallacarborane (cobalt bis(dicarbollide), Co(C2 B9 H11 )2 (2-) ) were developed. As metallacarborane donors, oxonium adducts of cobalt bis(dicarbollide) and 1,4-dioxane or tetrahydropyran were used. The physicochemical and biochemical properties of the obtained lysozyme-metallacarborane conjugates were studied for changes in secondary and tertiary structure, aggregation behavior, and biological activity. Only minor changes in primary, secondary, and tertiary protein structure were observed, caused by the single substitution of metallacarborane on lysozyme. However, the modification produced significant changes in lysozyme enzymatic activity and a tendency toward time- and temperature-dependent aggregation.

Keywords: boron cluster; conjugation; lysozyme; metallacarborane; protein modification.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Boron / chemistry*
  • Circular Dichroism
  • Cobalt / chemistry
  • Models, Molecular
  • Muramidase / chemistry*
  • Muramidase / metabolism*
  • Organometallic Compounds / chemical synthesis*
  • Protein Conformation
  • Protein Denaturation
  • Protein Stability
  • Solid-Phase Synthesis Techniques / methods
  • Spectrometry, Mass, Electrospray Ionization

Substances

  • Organometallic Compounds
  • Cobalt
  • Muramidase
  • Boron