Surface chemistry of graphene tailoring the activity of digestive enzymes by modulating interfacial molecular interactions

Tang, Huan1,2; Yang, Tong3; Chen, Lin1,2; Zhang, Ying1,2; Zhu, Yinhua1,2; Wang, Chen1,2; Liu, Dandan1,2; Guo, Qiuyan1,2; Cheng, Guangqing1,2; Xia, Fei1,2; Zhong, Tianyu3; Wang, Jigang1,2,4,5

2023-01-15

10.1016/j.jcis.2022.10.030

JOURNAL OF COLLOID AND INTERFACE SCIENCE   Impact Factor & Quartile

0021-9797

1095-7103

As a kind of novel functional material, graphene-related nanomaterials (GRMs) have great potentials in industrial and biomedical applications. Meanwhile, the production and wide application of GRMs will increase the risk of unintended or intentional oral exposure to human beings, attracting safety concerns about their biological fates and toxicological effects. The normal enzymatic activity of digestive enzymes is essential for the proper functioning of the gastrointestinal tract system. However, whether and how orally entered GRMs and their surface groups affect digestive enzymes' activity are still scarce. In this paper, we systematically studied the effects of graphene oxide (GO), graphene modified with hydroxyl groups (OH-G), carboxyl groups (COOH-G), and amino groups (NH2-G) on enzymatic activity of three typical digestive enzymes (pepsin, trypsin, and a-pancreatic amylase). The results showed that the activity of trypsin and a-pancreatic amylase could be greatly changed after GRMs incubation in a surface chemistry dependent manner, while the activity of pepsin was not affected. To elucidate the mechanisms at the molecular level, the interactions between trypsin and GRMs were studied by spectrometry, thermophoresis, and computational simulation approaches, and the key roles of surface chemistry of GRMs in tailoring the activity of trypsin were finally figured out. GO allosterically inhibited trypsin's activity in the non-competitive manner because of the conformation transition induced by the intensive interactions. COOH-G could effectively hamper enzymatic activity of trypsin in the competitive manner by blocking the active catalytic pocket. As for NH2-G and OH-G, they had little impact on the activity of trypsin due to the weak binding affinity or limited conformational change. Our findings not only indicate

Graphene Surface chemistry Enzymes Nano-bio interface Bio-effect of nanomaterials

SCI

English

Corresponding

National Key Research and Development Program of China[2020YFA0908000] ; National Key R&D Program of China[2020YFE0205100] ; Innovation Team and Talents Cultivation Program of the National Administration of Traditional Chinese Medicine[ZYYCXTD-C-202002] ; National Natural Science Foundation of China["82141001","82074098"] ; CACMS Innovation Fund["ZZ14-YQ-061","ZZ14-YQ-050"] ; Fundamental Research Funds for the Central public welfare research institutes["ZZ14-YQ-061","ZZ14-YQ-050","ZZ14-ND-010","ZZ15-ND-10","ZZ14-FL-002"]

Chemistry

Chemistry, Physical

WOS:000882145500007

ACADEMIC PRESS INC ELSEVIER SCIENCE

CHEMISTRY

Web of Science

1.China Acad Chinese Med Sci, Artemisinin Res Ctr, Beijing 100700, Peoples R China
2.Inst Chinese Mat Med, China Acad Chinese Med Sci, Beijing 100700, Peoples R China
3.Gannan Med Univ, Affiliated Hosp 1, Dept Lab Med, Ganzhou 341000, Jiangxi, Peoples R China
4.Southern Univ Sci & Technol, Shenzhen Peoples Hosp, Affiliated Hosp 1, Dept Nephrol, Shenzhen 518020, Guangdong, Peoples R China
5.Southern Med Univ, Dongguan Maternal & Child Hlth Care Hosp, Ctr Reprod Med, Dongguan 523125, Guangdong, Peoples R China

Tang, Huan,Yang, Tong,Chen, Lin,et al. Surface chemistry of graphene tailoring the activity of digestive enzymes by modulating interfacial molecular interactions[J]. JOURNAL OF COLLOID AND INTERFACE SCIENCE,2023,630.

Tang, Huan.,Yang, Tong.,Chen, Lin.,Zhang, Ying.,Zhu, Yinhua.,...&Wang, Jigang.(2023).Surface chemistry of graphene tailoring the activity of digestive enzymes by modulating interfacial molecular interactions.JOURNAL OF COLLOID AND INTERFACE SCIENCE,630.

Tang, Huan,et al."Surface chemistry of graphene tailoring the activity of digestive enzymes by modulating interfacial molecular interactions".JOURNAL OF COLLOID AND INTERFACE SCIENCE 630(2023).