scholarly journals Highly efficient H2S scavengers via thiolysis of positively-charged NBD amines

2020 ◽  
Vol 11 (30) ◽  
pp. 7823-7828 ◽  
Author(s):  
Ismail Ismail ◽  
Zhuoyue Chen ◽  
Lu Sun ◽  
Xiuru Ji ◽  
Haishun Ye ◽  
...  
Keyword(s):  
Live Cells ◽  
Highly Efficient ◽  
Positively Charged

We demonstrate that positively-charged NBD amines can effectively scavenge biological H2S in live cells and in mice.

Proximity Enzymatic Glyco-Remodeling Enables Direct and Highly Efficient Lipid Raft Imaging on Live Cells

2020 ◽  
Vol 92 (10) ◽  
pp. 7232-7239
Author(s):  
Jing Tao ◽  
Xiaofei Yu ◽  
Yuna Guo ◽  
Guyu Wang ◽  
Huangxian Ju ◽  
...  
Keyword(s):  
Lipid Raft ◽  
Live Cells ◽  
Highly Efficient

scholarly journals VDAC oligomers form mitochondrial pores to release mtDNA fragments and promote lupus-like disease

Science ◽  
2019 ◽  
Vol 366 (6472) ◽  
pp. 1531-1536 ◽  
Author(s):  
Jeonghan Kim ◽  
Rajeev Gupta ◽  
Luz P. Blanco ◽  
Shutong Yang ◽  
Anna Shteinfer-Kuzmine ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Lupus Erythematosus ◽  
Anion Channel ◽  
Live Cells ◽  
Mitochondrial Outer Membrane ◽  
Voltage Dependent Anion Channel ◽  
Mitochondrial Outer Membrane Permeabilization ◽  
Extracellular Traps ◽  
Voltage Dependent ◽  
Positively Charged

Mitochondrial stress releases mitochondrial DNA (mtDNA) into the cytosol, thereby triggering the type Ι interferon (IFN) response. Mitochondrial outer membrane permeabilization, which is required for mtDNA release, has been extensively studied in apoptotic cells, but little is known about its role in live cells. We found that oxidatively stressed mitochondria release short mtDNA fragments via pores formed by the voltage-dependent anion channel (VDAC) oligomers in the mitochondrial outer membrane. Furthermore, the positively charged residues in the N-terminal domain of VDAC1 interact with mtDNA, promoting VDAC1 oligomerization. The VDAC oligomerization inhibitor VBIT-4 decreases mtDNA release, IFN signaling, neutrophil extracellular traps, and disease severity in a mouse model of systemic lupus erythematosus. Thus, inhibiting VDAC oligomerization is a potential therapeutic approach for diseases associated with mtDNA release.

Hybrids of a 9-anthracenyl moiety and fluorescein as chemodosimeters for the detection of singlet oxygen in live cells

2019 ◽  
Vol 17 (46) ◽  
pp. 9883-9891 ◽  
Author(s):  
Serghei Chercheja ◽  
Steffen Daum ◽  
Hong-Gui Xu ◽  
Frank Beierlein ◽  
Andriy Mokhir
Keyword(s):  
Singlet Oxygen ◽  
Live Cells ◽  
Highly Efficient

A highly efficient fluorogenic chemodosimeter for the detection of singlet oxygen was developed.

Positively charged graphene oxide nanoparticle: precisely label the plasma membrane of live cell and sensitively monitor extracellular pH in situ

2014 ◽  
Vol 50 (28) ◽  
pp. 3695-3698 ◽  
Author(s):  
Huarui Zhu ◽  
Liang Gao ◽  
Xinglu Jiang ◽  
Ru Liu ◽  
Yueteng Wei ◽  
...  
Keyword(s):  
Graphene Oxide ◽  
Plasma Membrane ◽  
Positive Charge ◽  
Extracellular Ph ◽  
Live Cells ◽  
Oxide Nanoparticles ◽  
Ph Variation ◽  
Oxide Nanoparticle ◽  
Positively Charged

Graphene oxide nanoparticles with positive charge can be developed as fluorescent nanoprobes to detect extracellular pH variation of live cells.

Positively Charged Polysulfonamide Nanocomposite Membranes Incorporating Hydrophilic Triazine-Structured COFs for Highly Efficient Nanofiltration

2020 ◽  
Vol 3 (9) ◽  
pp. 9329-9339
Author(s):  
Heyun Wang ◽  
Hao Wang ◽  
Haoji Jiang ◽  
Ao Sheng ◽  
Zhong Wei ◽  
...  
Keyword(s):  
Nanocomposite Membranes ◽  
Highly Efficient ◽  
Positively Charged

Highly Efficient Exclusion of Alkali Metal Ions via Electrostatic Repulsion Inside Positively Charged Channels

Nano Letters ◽  
2020 ◽  
Vol 20 (5) ◽  
pp. 3627-3632
Author(s):  
Chenyang Zhang ◽  
Jun Tian ◽  
Shuaiwei Qi ◽  
Bing Yang ◽  
Zeyuan Dong
Keyword(s):  
Alkali Metal ◽  
Metal Ions ◽  
Alkali Metal Ions ◽  
Electrostatic Repulsion ◽  
Highly Efficient ◽  
Positively Charged

Protamine-DNA interaction

1978 ◽  
Vol 36 (2) ◽  
pp. 200-201
Author(s):  
D.P. Bazett-Jones ◽  
F.P. Ottensmeyer
Keyword(s):  
Small Volume ◽  
Double Helix ◽  
Dna Interaction ◽  
Dark Field ◽  
Sperm Head ◽  
Nuclear Proteins ◽  
Field Electron Microscopy ◽  
Dark Field Electron ◽  
Dna Double Helix ◽  
Positively Charged

Dark field electron microscopy has been used for the study of the structure of individual macromolecules with a resolution to at least the 5Å level. The use of this technique has been extended to the investigation of structure of interacting molecules, particularly the interaction between DNA and fish protamine, a class of basic nuclear proteins of molecular weight 4,000 daltons.Protamine, which is synthesized during spermatogenesis, binds to chromatin, displaces the somatic histones and wraps up the DNA to fit into the small volume of the sperm head. It has been proposed that protamine, existing as an extended polypeptide, winds around the minor groove of the DNA double helix, with protamine's positively-charged arginines lining up with the negatively-charged phosphates of DNA. However, viewing protamine as an extended protein is inconsistent with the results obtained in our laboratory.

Structure and Interaction of Protamine by Dark Field Electron Microscopy

1976 ◽  
Vol 34 ◽  
pp. 160-161
Author(s):  
D.P. Bazett-Jones ◽  
F.P. Ottensmeyer
Keyword(s):  
Electron Microscopy ◽  
Dark Field ◽  
Amino Acid Sequences ◽  
Dimensional Structure ◽  
3 Dimensional ◽  
Field Electron ◽  
Proposed Model ◽  
Field Electron Microscopy ◽  
Dark Field Electron ◽  
Positively Charged

It has been shown for some time that it is possible to obtain images of small unstained proteins, with a resolution of approximately 5Å using dark field electron microscopy (1,2). Applying this technique, we have observed a uniformity in size and shape of the 2-dimensional images of pure specimens of fish protamines (salmon, herring (clupeine, Y-l) and rainbow trout (Salmo irideus)). On the basis of these images, a model for the 3-dimensional structure of the fish protamines has been proposed (2).The known amino acid sequences of fish protamines show stretches of positively charged arginines, separated by regions of neutral amino acids (3). The proposed model for protamine structure (2) consists of an irregular, right-handed helix with the segments of adjacent arginines forming the loops of the coil.

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