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Peptoid-based Positional Scanning Derivatives: Revealing the Optimum ResidueRequired for Ice Recrystallization Inhibition Activity for Every Position in the AFGPs

Cited 5 time in scopus
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Title
Peptoid-based Positional Scanning Derivatives: Revealing the Optimum ResidueRequired for Ice Recrystallization Inhibition Activity for Every Position in the AFGPs
Other Titles
환형 결빙방지펩타이드 및 유사체의 얼음재결정화 활성
Authors
Ravichandran N. Murugan
Ahn, Mija
Shin, Song Yub
Bang, Jeong Kyu
Kim, Hak Jun
Subject
Chemistry
Keywords
glycopeptoid; ice recrystallization inhibiti; positional scanning
Issue Date
2012
Publisher
대한화학회
Citation
Ravichandran N. Murugan, et al. 2012. "Peptoid-based Positional Scanning Derivatives: Revealing the Optimum ResidueRequired for Ice Recrystallization Inhibition Activity for Every Position in the AFGPs". BULLETIN OF THE KOREAN CHEMICAL SOCIETY, 33(12): 3931-3932.
Abstract
Antifreeze glycoproteins (AFGPs) bind to the ice crystals, thereby inhibit ice crystal growth. The discovery of AFGPs in the blood serum of fish by De Vries demonstrated that AFGPs is an essential biomaterial for fish to survive at subzero temperature in the Antarctic Sea1. This unique property of AFGPs has attracted significant interest due to their potential application in a variety of fields including medicine and the frozen-food industry. AFGPs were classified into 8 subclasses, in which AFGP1 has the largest (33.7 kDa), and AFGP8 has the lowest molecular weight fraction (2.6 kDa). Among AFGPs, AFGP8 is good candidate as biomaterial due to the lowest molecular weight (2.6 kDa) that led to the intensive studies on the synthesis and activity of AFGP8-related compounds by several research groups2, to develop efficient and cost-effective mass production of AFGPs with high purity as well as to understand the mechanism of action of AFGP8. AFGP8 was consists of repeating tripeptide units, Alanyl-Alanyl-Threonyl (Ala-Ala-Thr)n=4 units, connected with the disaccharide β-D-galactosyl-(1→3)-α-D-N-acetylgalactosamine through a glycosidic bond at the hydroxyl group of the threonine residue.ero temperature in the Antarctic Sea1. This unique property of AFGPs has attracted significant interest due to their potential application in a variety of fields including medicine and the frozen-food industry. AFGPs were classified into 8 subclasses, in which AFGP1 has the largest (33.7 kDa), and AFGP8 has the lowest molecular weight fraction (2.6 kDa). Among AFGPs, AFGP8 is good candidate as biomaterial due to the lowest molecular weight (2.6 kDa) that led to the intensive studies on the synthesis and activity of AFGP8-related compounds by several research groups2, to develop efficient and cost-effective mass production of AFGPs with high purity as well as to understand the mechanism of action of AFGP8. AFGP8 was consists of repeating tripeptide
URI
http://repository.kopri.re.kr/handle/201206/6550
DOI
http://dx.doi.org/10.5012/bkcs.2012.33.12.3931
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