• 文献标题:   Control of the Graphene-Protein Interface Is Required To Preserve Adsorbed Protein Function
  • 文献类型:   Article
  • 作  者:   ALAVA T, MANN JA, THEODORE C, BENITEZ JJ, DICHTEL WR, PARPIA JM, CRAIGHEAD HG
  • 作者关键词:  
  • 出版物名称:   ANALYTICAL CHEMISTRY
  • ISSN:   0003-2700 EI 1520-6882
  • 通讯作者地址:   Cornell Univ
  • 被引频次:   68
  • DOI:   10.1021/ac303268z
  • 出版年:   2013

▎ 摘  要

Graphene's suite of useful properties makes it of interest for use in biosensors. However, graphene interacts strongly with hydrophobic components of biomolecules, potentially altering their conformation and disrupting their biological activity. We have immobilized the protein Concanavalin A onto a self-assembled monolayer of multivalent tripodal molecules on single-layer graphene. We used a quartz crystal microbalance (QCM) to show that tripod-bound Concanavalin A retains its affinity for polysaccharides containing alpha-D-glucopyrannosyl groups as well as for the alpha-D-mannopyranosyl groups located on the cell wall of Bacillus subtilis. QCM measurements on unfunctionalized graphene indicate that adsorption of Concanavalin A onto graphene is accompanied by near-complete loss of these functions, suggesting that interactions with the graphene surface induce deleterious structural changes to the protein. Given that Concanavalin A's tertiary structure is thought to be relatively robust, these results suggest that other proteins might also be denatured upon adsorption onto graphene, such that the graphene-biomolecule interface must be considered carefully. Multivalent tripodal binding groups address this challenge by anchoring proteins without loss of function and without disrupting graphene's desirable electronic structure.