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Synthesis of Cyclic Antifreeze Glycopeptide and Glycopeptoids and Their Ice Recrystallization Inhibition Activity

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Title
Synthesis of Cyclic Antifreeze Glycopeptide and Glycopeptoids and Their Ice Recrystallization Inhibition Activity
Other Titles
Antifreeze Glycopeptide 유도체 합성 및 합성된 물질의 결빙방지활성 측정
Authors
Ravichandran N. Murugan
Kim, Eunjung
Jeong Kyu Bang
Kim, Hak Jun
Mija Ahn
Lee, Jun Hyuck
Song Yub Shin
Subject
Chemistry
Keywords
Cyclic glycopeptide; Cyclic glycopeptoid; Ice recrystallization inhibiti; Solid phase synthesis
Issue Date
2012
Publisher
Korean Chemical Society
Citation
Ravichandran N. Murugan, et al. 2012. "Synthesis of Cyclic Antifreeze Glycopeptide and Glycopeptoids and Their Ice Recrystallization Inhibition Activity". BULLETIN OF THE KOREAN CHEMICAL SOCIETY, 33(11): 3565-3570.
Abstract
Until now, few groups reported the antifreeze activity of cyclic glycopeptides;however, the tedious synthetic procedure is not amenable to study the intensive structure activity relationship. A series of N-linked cyclic glycopeptoids and glycopeptide have been prepared to evaluate antifreeze activity as a function of peptide backbone cyclization and methyl stereochemical effect on the rigid Thr position. This study has combined the cyclization protocol with solid phase peptide synthesis and obtained significant quantities of homogeneous cyclic glycopeptide and glycopeptoids. Analysis of antifreeze activity revealed that our cyclic peptide demonstrated RI activity while cyclic glycopeptoids showed no RI activity. These results suggest that the subtle changes in conformation and Thr orientation dramatically influence RI activity of N-linked glycopeptoidsnd glycopeptide have been prepared to evaluate antifreeze activity as a function of peptide backbone cyclization and methyl stereochemical effect on the rigid Thr position. This study has combined the cyclization protocol with solid phase peptide synthesis and obtained significant quantities of homogeneous cyclic glycopeptide and glycopeptoids. Analysis of antifreeze activity revealed that our cyclic peptide demonstrated RI activity while cyclic glycopeptoids showed no RI activity. These results suggest that the subtle changes in conformation and Thr orientation dramatically influence RI activity of N-linked glycopeptoids
URI
http://repository.kopri.re.kr/handle/201206/6549
DOI
http://dx.doi.org/10.5012/bkcs.2012.33.11.3565
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