Effects antifreeze peptides on the thermotropic properties of a model membrane

Hagit Kun, Refael Minnes, Yitzhak Mastai

Research output: Contribution to journalArticlepeer-review

10 Scopus citations


In this paper, we report on the effect of short segments of type I antifreeze protein (AFP I) on the thermotropic properties of a model membrane. Two different types of dimyristoylphosphatidylcholine model membranes were used, multilamellar vesicles and small unilamellar vesicles. The membrane properties were studied by differential scanning calorimetry (DSC) and fluorescence anisotropy. With the incorporation of AFP I and its short segments, the order of the model membrane increased both in the gel state and in the liquid crystalline state. The interaction of AFPs with the model membrane caused a shift in the phase transition to lower temperatures, which is accompanied by a broadening of the DSC thermogram. This preferential stabilization to a more ordered phase by the AFPs could be due to ordering the hydrophobic membrane core and separation into domains. Overall, this approach of employing short segments of AFP I simplifies the correlation between antifreeze protein characteristics and the effect of these parameters on the interaction mechanism of AFP with cell membranes. The success of this approach can lead to the identification of short peptides with high antifreeze activity.

Original languageEnglish
Pages (from-to)389-396
Number of pages8
JournalJournal of Bioenergetics and Biomembranes
Issue number4
StatePublished - Aug 2008

Bibliographical note

Funding Information:
Acknowledgments Y. Mastai acknowledges financial support from Horvitz Foundation. We thank Prof. Meir Shinitzky from the Weizmann Institute of Science and Prof. Benjamin Ehrenberg form the department of Physics Bar Ilan University for useful discussions.


  • Antifreeze peptides
  • Model membrane
  • Peptide-lipid interactions
  • Thermotropic properties


Dive into the research topics of 'Effects antifreeze peptides on the thermotropic properties of a model membrane'. Together they form a unique fingerprint.

Cite this