Functional importance of short-range binding and long-range solvent interactions in helical antifreeze peptides

Simon Ebbinghaus, Konrad Meister, Maxim B. Prigozhin, Arthur L. Devries, Martina Havenith, Joachim Dzubiella, Martin Gruebele

Research output: Contribution to journalArticle

Abstract

Short-range ice binding and long-range solvent perturbation both have been implicated in the activity of antifreeze proteins and antifreeze glycoproteins. We study these two mechanisms for activity of winter flounder antifreeze peptide. Four mutants are characterized by freezing point hysteresis (activity), circular dichroism (secondary structure), Förster resonance energy transfer (end-to-end rigidity), molecular dynamics simulation (structure), and terahertz spectroscopy (long-range solvent perturbation). Our results show that the short-range model is sufficient to explain the activity of our mutants, but the long-range model provides a necessary condition for activity: the most active peptides in our data set all have an extended dynamical hydration shell. It appears that antifreeze proteins and antifreeze glycoproteins have reached different evolutionary solutions to the antifreeze problem, utilizing either a few precisely positioned OH groups or a large quantity of OH groups for ice binding, assisted by long-range solvent perturbation.

Original languageEnglish (US)
Pages (from-to)L20-L22
JournalBiophysical journal
Volume103
Issue number2
DOIs
StatePublished - Jul 18 2012

ASJC Scopus subject areas

  • Biophysics

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