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제109회 대한화학회 학술발표회, 총회 및 기기전시회 안내 An efficient solidphase synthesis of glycopeptide with various valences and different spatial arrangements of the sugar and analysis of density dependent binding of glycan

2012년 2월 16일 21시 11분 11초
ORGN.P-921 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
4월 25일 (수요일) 18:00~21:00
저자 및
배재영, 신인재
연세대학교 화학과, Korea

Recognition of glycans present in the form of glycoconjugates (e.g. glycoproteins, glycosphingolipids, proteoglycans) in cells by proteins is a crucial biological event that is implicated in various physiological and pathological processes. Thus, understanding the role of glycan-mediated recognition events and blocking glycan-protein interactions associated with diseases, such as inflammation, cancer and pathogen infection, are of great importance for biological research and therapeutic applications. Typically, carbohydrate-binding proteins (lectins) interact with monovalent sugars with weak binding affinity (millimolar range) and poor selectivity. A facile and efficient solidphase synthesis of linear peptide-based glycoclusters with various valences and different spatial arrangements of the sugar ligands is described. Lectin binding properties of the glycoclusters were initially examined by using microarrays immobilized by various lectins. These glycoclusters were then employed to detect the cell-surface carbohydrate- binding proteins in bacteria. Finally, the uptake of glycoclusters by mammalian cells through receptormediated endocytosis was evaluated. The results, obtained from the in vitro and in vivo studies, indicate that the binding affinities toward immobilized and cell-surface proteins are highly dependent on the valence and spatial arrangements of the sugar ligands in glycoclusters.