Acta Phys. -Chim. Sin. ›› 2017, Vol. 33 ›› Issue (2): 426-434.doi: 10.3866/PKU.WHXB201609291

• ARTICLE • Previous Articles     Next Articles

Preparation and Characterization of Dithiocarbamate Based Carbohydrate Chips

Fang CHENG1,2,*(),Han-Qi WANG1,2,Kuang XU1,2,Wei HE3   

  1. 1 State Key Laboratory of Fine Chemicals, Dalian University of Technology, Dalian 116023, Liaoning Province, P. R. China
    2 School of Pharmaceutical Science and Technology, Dalian University of Technology, Dalian 116023, Liaoning Province, P. R. China
    3 School of Chemical Engineering, Dalian University of Technology, Dalian 116023, Liaoning Province, P. R. China
  • Received:2016-08-12 Published:2017-01-12
  • Contact: Fang CHENG
  • Supported by:
    the National Natural Science Foundation of China(21104008,21231003);Fundamental Research Funds for the Central Universities, China and Recruitment Program of Global Youth Experts, China(DUT16RC(3)019)


Carbohydrates chips are powerful tools for quantitatively studying protein-carbohydrate interactions. Typically, carbohydrate chips are prepared using the self-assembly of carbohydrate thiol/disulfide, which always requires multiple hydroxyl group protection/deprotection steps resulting low conversion in the preparation. In this paper, a kind of carbohydrate derivatives containing dithiocarbamate (DTC) group was synthesized through a two-step reaction to prepare self-assembled monolayers presenting carbohydrate (glycol-DTC SAMs). The glycol-DTC SAMs was characterized using X-ray photoelectron spectroscopy (XPS) and the protein binding activity was quantitatively analysized using surface plasma resonance (SPR) and enzyme linked lectin assay (ELLA). By mixed self-assembly of carbohydrate dithiocarbamate and sarcosine dithiocarbamate, Glycol-DTC SAMs with different glucose density were prepared. The protein binding kinetics was monitored in real time and the thermodynamics was calculated. Interestingly, a 1:1 binding of concanavalin A (Con A) was obtained on the SAMs prepared in solution containing 1% glucose-DTC, as the dissociation constant (Kd) was calculated to be (39.10±0.12) μmol·L-1. A 1:2 binding of Con A was obtained on the SAMs prepared in solutions containing >2% glucose-DTC, as the Kd was calculated to be (1.17±0.18) μmol·L-1. By simply mixed selfassembly, multivalent binding of Con A can be realized and separate kinetic parameters can be obtained. Our work would promote the study of protein-carbohydrate interactions and be helpful for revealing the relevant biological progress.

Key words: Carbohydrate-protein interaction, Dithiocarbamate, Multivalent adsorption, Thermodynamics, Kinetics, SAM