NAMI-A preferentially reacts with the Sp1 protein: understanding the anti-metastasis effect of the drug

Siming Yuan; Siming Chen; Han Wu; Huan Jiang; Shihui Zheng; Qianling Zhang; Yangzhong Liu

doi:10.1039/c9cc08775c

NAMI-A preferentially reacts with the Sp1 protein: understanding the anti-metastasis effect of the drug

Chem Commun (Camb). 2020 Jan 30;56(9):1397-1400. doi: 10.1039/c9cc08775c.

Authors

Siming Yuan¹, Siming Chen, Han Wu, Huan Jiang, Shihui Zheng, Qianling Zhang, Yangzhong Liu

Affiliation

¹ Shenzhen Key Laboratory for Functional Polymer, College of Chemistry and Environmental Engineering, Shenzhen University, Shenzhen, Guangdong 518060, China. zhql@szu.edu.cn.

PMID: 31912815
DOI: 10.1039/c9cc08775c

Abstract

NAMI-A is highly reactive to Sp1, a tumor metastasis related protein, resulting in the perturbation of the protein structure and disruption of the DNA recognition of Sp1. Interestingly, Sp1 is more susceptible than other zinc finger proteins to NAMI-A, suggesting that Sp1 could be the anti-metastasis target of NAMI-A.

MeSH terms

Antineoplastic Agents / chemistry*
DNA / metabolism
Dimethyl Sulfoxide / analogs & derivatives*
Dimethyl Sulfoxide / chemistry
Glutathione / chemistry
Organometallic Compounds / chemistry*
Protein Binding
Protein Multimerization / drug effects
Protein Structure, Secondary / drug effects
Protein Unfolding / drug effects
Ruthenium Compounds / chemistry*
Sp1 Transcription Factor / chemistry*
Sp1 Transcription Factor / metabolism

Substances

Antineoplastic Agents
Organometallic Compounds
Ruthenium Compounds
Sp1 Transcription Factor
imidazolium-bis(imidazole)dimethylsulfoxideimidazotetrachlororuthenate(III)
DNA
Glutathione
Dimethyl Sulfoxide