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Latent ice recrystallization inhibition activity in nonantifreeze proteins : Ca2+-activated plant lectins and cation-activated antimicrobial peptides
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Mitchell, Daniel E. and Gibson, Matthew I. (2015) Latent ice recrystallization inhibition activity in nonantifreeze proteins : Ca2+-activated plant lectins and cation-activated antimicrobial peptides. Biomacromolecules, 16 (10). pp. 3411-3416. doi:10.1021/acs.biomac.5b01118
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Official URL: http://dx.doi.org/10.1021/acs.biomac.5b01118
Abstract
Organisms living in polar regions have evolved a series of antifreeze (glyco) proteins (AFGPs) to enable them to survive by modulating the structure of ice. These proteins have huge potential for use in cellular cryopreservation, ice-resistant surfaces, frozen food, and cryosurgery, but they are limited by their relatively low availability and questions regarding their mode of action. This has triggered the search for biomimetic materials capable of reproducing this function. The identification of new structures and sequences capable of inhibiting ice growth is crucial to aid our understanding of these proteins. Here, we show that plant c-type lectins, which have similar biological function to human c-type lectins (glycan recognition) but no sequence homology to AFPs, display calcium-dependent ice recrystallization inhibition (IRI) activity. This IRI activity can be switched on/off by changing the Ca2+ concentration. To show that more (nonantifreeze) proteins may exist with the potential to display IRI, a second motif was considered, amphipathicity. All known AFPs have defined hydrophobic/hydrophilic domains, rationalizing this choice. The cheap, and widely used, antimicrobial Nisin was found to have cation-dependent IRI activity, controlled by either acid or addition of histidine-binding ions such as zinc or nickel, which promote its amphipathic structure. These results demonstrate a new approach in the identification of antifreeze protein mimetic macromolecules and may help in the development of synthetic mimics of AFPs.
| Item Type: | Journal Article | ||||||||
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| Subjects: | Q Science > QP Physiology | ||||||||
| Divisions: | Faculty of Science > Chemistry | ||||||||
| Library of Congress Subject Headings (LCSH): | Antifreeze proteins, Glycoproteins | ||||||||
| Journal or Publication Title: | Biomacromolecules | ||||||||
| Publisher: | American Chemical Society | ||||||||
| ISSN: | 1525-7797 | ||||||||
| Official Date: | 12 October 2015 | ||||||||
| Dates: |
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| Volume: | 16 | ||||||||
| Number: | 10 | ||||||||
| Number of Pages: | 6 | ||||||||
| Page Range: | pp. 3411-3416 | ||||||||
| DOI: | 10.1021/acs.biomac.5b01118 | ||||||||
| Status: | Peer Reviewed | ||||||||
| Publication Status: | Published | ||||||||
| Access rights to Published version: | Open Access | ||||||||
| Funder: | Advantage West Midlands (AWM), European Regional Development Fund (ERDF), Royal Society (Great Britain), Engineering and Physical Sciences Research Council (EPSRC), Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC), European Research Council (ERC) | ||||||||
| Grant number: | EP/F500378/1 (EPSRC), BB/F011199/ 1 (BBSRC), CRYOMAT 638661 (ERC) |
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