Earticle

초록

영어

Enzymatic glycosylation on solid surface is an efficient and useful tool to improve the limitation of conventional glycan synthesis and provide diverse glycan sources to use for analyzing glycan-protein interaction on surface. In this work, a novel glycan microarray platform introduced glycan-oligonucleotide conjugates was developed to prepare glycan sources for analyzing glycan-protein interactions through solid surface based-enzymatic glycan synthesis. Pasteurella multocida sialyltrnasferase (PmST), Campylobacter jejuni N-acetylgalactosaminyltransferase (CgtA), and C. jejuni galactosyltransferase (CgtB) were taken as target enzymes to synthesize GM1-related glycans such as GM1 pentasaccharide, GM2 tetrasaccharide, and GM3 trisaccharide. HPLC analysis showed that three glycosyltrnasferases expressed in Escherichia coli were produced as active forms. Synthesized glycans on this platform could be effectively obtained through DNA denaturation process under appropriate condition and identified by mass measurement. We anticipate that this novel glycan microarray platform combining enzymatic glycosylation with mass measurement can serve a solution to improve the difficulty of obtaining glycan sources and provide a new direction toward studies about glycan synthesis and glycan-related diverse interaction analysis.

저자

• Hye Ryoung Heo [ Department of Chemical Engineering, Pohang University of Science and Technology ]
• Chang Sup Kim [ Department of Chemical Engineering, Pohang University of Science and Technology, School of Chemistry and Biochemistry, Yeungnam University ]
• Jeong Hyun Seo [ Department of Chemical Engineering, Pohang University of Science and Technology, School of Chemical Engineering, Yeungnam University ]
• Hyung Joon Cha [ Department of Chemical Engineering, Pohang University of Science and Technology ]

참고문헌

발행기관

간행물

표지보기 관심저널 등록

• 간행물명

  한국당과학회 학술대회

• 간기

  연간

• 수록기간

  2006~2022

• 십진분류

  KDC 517 DDC 614