Modular functionalization of crystalline graphene by recombinant proteins: a nanoplatform for probing biomolecules

Abhishek Tyagi, Xiaotian Liu, Irfan Haider Abidi, Zhaoli Gao, Byung Min Park, Xiangze Zeng, Xuewu Ou, Aldrine Abenoja Cagang, Minghao Zhuang, Md Delowar Hossain, Kai Zhang, Lu Tao Weng*, Fei Sun*, Zhengtang Luo*

*Corresponding author for this work

Research output: Contribution to journalJournal articlepeer-review

11 Citations (Scopus)

Abstract

Graphene, as well as other two-dimensional materials, is a promising candidate for use in bioimaging, therapeutic drug delivery, and bio-sensing applications. Here, we developed a protocol to functionalize graphene with recombinant proteins using genetically encoded SpyTag-SpyCatcher chemistry. SpyTag forms a covalent isopeptide bond with its genetically encoded partner SpyCatcher through spontaneous amidation under physiological conditions. The functionalization protocol developed is based on the use of short proteins as a linker, where two graphene-binding-peptides (GBPs) are attached to both ends of SpyTag (referred to as GStG), followed by the covalent conjugation with SpyCatcher-fusion proteins. The proposed method enables the decoration of crystalline graphene with various proteins, such as fluorescent proteins and affibody molecules that bind to cancerous cells. This scheme, which takes advantage of the cleanness of single-crystal graphene and the robustness of SpyTag-SpyCatcher chemistry, provides a versatile platform on which to study the biomolecule-surface and cell-substrate interactions and, indeed, may lead to a new way of designing biomedical devices. The interaction between peptides and graphene was clearly shown using molecular dynamics simulation and proven using specially designed experiments.

Original languageEnglish
Pages (from-to)22572-22582
Number of pages11
JournalNanoscale
Volume10
Issue number47
DOIs
Publication statusPublished - 21 Dec 2018
Externally publishedYes

Scopus Subject Areas

  • Materials Science(all)

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