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Antifreeze Peptides and Glycopeptides, and Their Derivatives: Potential Uses in Biotechnology
Antifreeze proteins (AFPs) and glycoproteins (AFGPs), collectively called AF(G)Ps, constitute a diverse class of proteins found in various Arctic and Antarctic fish, as well as in amphibians, plants, and insects. These compounds possess the ability to inhibit the formation of ice and are therefore e...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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MDPI
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3721219/ https://www.ncbi.nlm.nih.gov/pubmed/23752356 http://dx.doi.org/10.3390/md11062013 |
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author | Bang, Jeong Kyu Lee, Jun Hyuck Murugan, Ravichandran N. Lee, Sung Gu Do, Hackwon Koh, Hye Yeon Shim, Hye-Eun Kim, Hyun-Cheol Kim, Hak Jun |
author_facet | Bang, Jeong Kyu Lee, Jun Hyuck Murugan, Ravichandran N. Lee, Sung Gu Do, Hackwon Koh, Hye Yeon Shim, Hye-Eun Kim, Hyun-Cheol Kim, Hak Jun |
author_sort | Bang, Jeong Kyu |
collection | PubMed |
description | Antifreeze proteins (AFPs) and glycoproteins (AFGPs), collectively called AF(G)Ps, constitute a diverse class of proteins found in various Arctic and Antarctic fish, as well as in amphibians, plants, and insects. These compounds possess the ability to inhibit the formation of ice and are therefore essential to the survival of many marine teleost fishes that routinely encounter sub-zero temperatures. Owing to this property, AF(G)Ps have potential applications in many areas such as storage of cells or tissues at low temperature, ice slurries for refrigeration systems, and food storage. In contrast to AFGPs, which are composed of repeated tripeptide units (Ala-Ala-Thr)(n) with minor sequence variations, AFPs possess very different primary, secondary, and tertiary structures. The isolation and purification of AFGPs is laborious, costly, and often results in mixtures, making characterization difficult. Recent structural investigations into the mechanism by which linear and cyclic AFGPs inhibit ice crystallization have led to significant progress toward the synthesis and assessment of several synthetic mimics of AFGPs. This review article will summarize synthetic AFGP mimics as well as current challenges in designing compounds capable of mimicking AFGPs. It will also cover our recent efforts in exploring whether peptoid mimics can serve as structural and functional mimics of native AFGPs. |
format | Online Article Text |
id | pubmed-3721219 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-37212192013-07-24 Antifreeze Peptides and Glycopeptides, and Their Derivatives: Potential Uses in Biotechnology Bang, Jeong Kyu Lee, Jun Hyuck Murugan, Ravichandran N. Lee, Sung Gu Do, Hackwon Koh, Hye Yeon Shim, Hye-Eun Kim, Hyun-Cheol Kim, Hak Jun Mar Drugs Review Antifreeze proteins (AFPs) and glycoproteins (AFGPs), collectively called AF(G)Ps, constitute a diverse class of proteins found in various Arctic and Antarctic fish, as well as in amphibians, plants, and insects. These compounds possess the ability to inhibit the formation of ice and are therefore essential to the survival of many marine teleost fishes that routinely encounter sub-zero temperatures. Owing to this property, AF(G)Ps have potential applications in many areas such as storage of cells or tissues at low temperature, ice slurries for refrigeration systems, and food storage. In contrast to AFGPs, which are composed of repeated tripeptide units (Ala-Ala-Thr)(n) with minor sequence variations, AFPs possess very different primary, secondary, and tertiary structures. The isolation and purification of AFGPs is laborious, costly, and often results in mixtures, making characterization difficult. Recent structural investigations into the mechanism by which linear and cyclic AFGPs inhibit ice crystallization have led to significant progress toward the synthesis and assessment of several synthetic mimics of AFGPs. This review article will summarize synthetic AFGP mimics as well as current challenges in designing compounds capable of mimicking AFGPs. It will also cover our recent efforts in exploring whether peptoid mimics can serve as structural and functional mimics of native AFGPs. MDPI 2013-06-10 /pmc/articles/PMC3721219/ /pubmed/23752356 http://dx.doi.org/10.3390/md11062013 Text en © 2013 by the authors; licensee MDPI, Basel, Switzerland. http://creativecommons.org/licenses/by/3.0/ This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/). |
spellingShingle | Review Bang, Jeong Kyu Lee, Jun Hyuck Murugan, Ravichandran N. Lee, Sung Gu Do, Hackwon Koh, Hye Yeon Shim, Hye-Eun Kim, Hyun-Cheol Kim, Hak Jun Antifreeze Peptides and Glycopeptides, and Their Derivatives: Potential Uses in Biotechnology |
title | Antifreeze Peptides and Glycopeptides, and Their Derivatives: Potential Uses in Biotechnology |
title_full | Antifreeze Peptides and Glycopeptides, and Their Derivatives: Potential Uses in Biotechnology |
title_fullStr | Antifreeze Peptides and Glycopeptides, and Their Derivatives: Potential Uses in Biotechnology |
title_full_unstemmed | Antifreeze Peptides and Glycopeptides, and Their Derivatives: Potential Uses in Biotechnology |
title_short | Antifreeze Peptides and Glycopeptides, and Their Derivatives: Potential Uses in Biotechnology |
title_sort | antifreeze peptides and glycopeptides, and their derivatives: potential uses in biotechnology |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3721219/ https://www.ncbi.nlm.nih.gov/pubmed/23752356 http://dx.doi.org/10.3390/md11062013 |
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