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Antifreeze Peptides and Glycopeptides, and Their Derivatives: Potential Uses in Biotechnology

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Title
Antifreeze Peptides and Glycopeptides, and Their Derivatives: Potential Uses in Biotechnology
Other Titles
결빙방지(당)펩타이드와 이의 산업적 이용 (공동 제1저자)
Authors
Lee, Jun Hyuck
Kim, Hak Jun
Kim, Hyun-cheol
Shim, Hye-Eun
Koh, Hye Yeon
Do, Hackwon
Jeong Kyu Bang
Lee, Sung Gu
Ravichandran N. Murugan
Subject
Pharmacology & Pharmacy
Keywords
antifreeze glycopeptide; antifreeze protein; recrystallization inhibition; thermal hysteresis
Issue Date
2013
Publisher
MDPI
Citation
Lee, Jun Hyuck, et al. 2013. "Antifreeze Peptides and Glycopeptides, and Their Derivatives: Potential Uses in Biotechnology". Marine Drugs, 11(6): 2013-2041.
Abstract
Antifreeze proteins (AFPs) and glycoproteins (AFGPs), collectively called as 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.ess 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.
URI
http://repository.kopri.re.kr/handle/201206/5886
DOI
http://dx.doi.org/10.3390/md11062013
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