Journal
BULLETIN OF THE KOREAN CHEMICAL SOCIETY
Volume 33, Issue 11, Pages 3565-3570Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.5012/bkcs.2012.33.11.3565
Keywords
Cyclic glycopeptide; Ice recrystallization inhibition; Solid phase synthesis; Cyclic glycopeptoid
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Funding
- Korea Basic Science Institute's high field NMR research program grant [T3022B]
- Korea Research Council of Fundamental Science & Technology (KRCF)
- Korea Polar Research Institute (KOPRI) [PE11100]
- Korea Research Foundation
- Korean Government [KRF-2011-0009039]
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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 glycopeptoids
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