Dodine as a protein denaturant: The best of two worlds?

Hannah Gelman, Tatyana Perlova, Martin Gruebele

Research output: Contribution to journalArticlepeer-review


Traditional denaturants such as urea and guanidinium ion unfold proteins in a cooperative "all-or-none" fashion. However, their high working concentration in combination with their strong absorption in the far ultraviolet region make it impossible to measure high quality circular dichroism or infrared spectra, which are commonly used to detect changes in protein secondary structure. On the other hand, detergents such as dodecyl sulfate destabilize native protein conformation at low millimolar concentrations and are UV transparent, but they denature proteins more gradually than guanidinium or urea. In this work, we studied the denaturation properties of the fungicide dodecylguanidinium acetate (dodine), which combines both denaturants into one. We show that dodine unfolds some small proteins at millimolar concentrations, facilitates temperature denaturation, and is transparent enough at its working concentration, unlike guanidinium, to measure full range circular dichroism spectra. Our results also suggest that dodine allows fine-tuning of the protein's unfolded state, unlike traditional "all-or-none" denaturants.

Original languageEnglish (US)
Pages (from-to)13090-13097
Number of pages8
JournalJournal of Physical Chemistry B
Issue number42
StatePublished - Oct 24 2013

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Surfaces, Coatings and Films
  • Materials Chemistry


Dive into the research topics of 'Dodine as a protein denaturant: The best of two worlds?'. Together they form a unique fingerprint.

Cite this