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University of Massachusetts Amherst

Chemistry Department Faculty Publication Series

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Full-Text Articles in Other Physical Sciences and Mathematics

Effective And Selective Dna Modification On Bacterial Membranes, Qian Tian, Yousef Bagheri, Puspam Keshri, Rigumula Wu, Kewei Ren, Qikun Yu, Mingxu You Jan 2021

Effective And Selective Dna Modification On Bacterial Membranes, Qian Tian, Yousef Bagheri, Puspam Keshri, Rigumula Wu, Kewei Ren, Qikun Yu, Mingxu You

Chemistry Department Faculty Publication Series

With highly precise self-assembly and programmability, DNA has been widely used as a versatile material in nanotechnology and synthetic biology. Recently, DNA-based nanostructures and devices have been engineered onto eukaryotic cell membranes for various exciting applications in the detection and regulation of cell functions. While in contrast, the potential of applying DNA nanotechnology for bacterial membrane studies is still largely underexplored, which is mainly due to the lack of tools to modify DNA on bacterial membranes. Herein, using lipid-DNA conjugates, we have developed a simple, fast, and highly efficient system to engineer bacterial membranes with designer DNA molecules. We have …


Egcg Binds Intrinsically Disordered N-Terminal Domain Of P53 And Disrupts P53-Mdm2 Interaction, Jianhen Chen, Jing Zhao, Alan Blayney, Xiaorong Liu, Lauren Gandy, Weihua Jin, Lufeng Yan, Jeung-Hoi Ha, Ashley J. Canning, Michael Connelly Jan 2021

Egcg Binds Intrinsically Disordered N-Terminal Domain Of P53 And Disrupts P53-Mdm2 Interaction, Jianhen Chen, Jing Zhao, Alan Blayney, Xiaorong Liu, Lauren Gandy, Weihua Jin, Lufeng Yan, Jeung-Hoi Ha, Ashley J. Canning, Michael Connelly

Chemistry Department Faculty Publication Series

Epigallocatechin gallate (EGCG) from green tea can induce apoptosis in cancerous cells, but the underlying molecular mechanisms remain poorly understood. Using SPR and NMR, here we report a direct, mu M interaction between EGCG and the tumor suppressor p53 (K-D=1.61.4 mu M), with the disordered N-terminal domain (NTD) identified as the major binding site (K-D=4 +/- 2 mu M). Large scale atomistic simulations (>100 mu s), SAXS and AUC demonstrate that EGCG-NTD interaction is dynamic and EGCG causes the emergence of a subpopulation of compact bound conformations. The EGCG-p53 interaction disrupts p53 interaction with its regulatory E3 ligase MDM2 …