Antifreeze glycoprotein agents: Structural requirements for activity

Research output: Contribution to journalShort surveypeer-review

12 Scopus citations

Abstract

Antifreeze glycoproteins (AFGPs) are considered to be the most efficient means to reduce ice damage to cell tissues since they are able to inhibit growth and crystallization of ice. The key element of antifreeze proteins is to act in a non-colligative manner which allows them to function at concentrations 300-500 times lowers than other dissolved solutes. During the past decade, AFGPs have demonstrated tremendous potential for many pharmaceutical and food applications. Presently, the only route to obtain AFGPs involves the time consuming and expensive process of isolation and purification from deep-sea polar fishes. Unfortunately, it is not amenable to mass production and commercial applications. The lack of understanding of the mechanism through which the AFGPs inhibit ice growth has also hampered the realization of industrial and biotechnological applications. Here we report the structural motifs that are essential for antifreeze activity of AFGPs, and propose a unified mechanism based on both recent studies of short alanine peptides and structure activity relationship of synthesized AFGPs.

Original languageEnglish
Pages (from-to)2507-2510
Number of pages4
JournalJournal of the Science of Food and Agriculture
Volume91
Issue number14
DOIs
StatePublished - Nov 2011
Externally publishedYes

Keywords

  • AFGP
  • Antifreeze glycoprotein
  • Ice crystal inhibition
  • Poly-L-proline II
  • Protein hydration

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