JBC resolves unique new features of viral proteins

Rabbits are one of the few mammals that are resistant to infectious spongiform encephalopathies (TSE). Studies have shown that rabbit prion protein (PrPC) is different from most mammalian PrPC in that it does not undergo a conformational transition of PrPC→PrPSc, but its molecular mechanism is still unclear. It is expected to be closely related to the spatial structure and kinetics of rabbit PrPC protein. Related.

The researchers from the Shanghai Institute of Materia Medica of the Chinese Academy of Sciences used multidimensional NMR technology to study the solution structure and kinetics of rabbit PrPC (91-228) and its S173N and other point mutant proteins, and found that the rabbit PrPC protein has a unique spatial structure and Kinetic properties. The results of this research are published in the journal J. Biol. Chem.

Leading the research is Lin Donghai, a researcher at the Shanghai Institute of Materia Medica, Chinese Academy of Sciences. He graduated from Xiamen University in the early years and studied at the National Nuclear Magnetic Resonance Laboratory of the City of Hope National Medical Center in the United States. In 2002, he was elected to the Chinese Academy of Sciences. "In June 2003, he returned to China and worked at the Shanghai Institute of Materia Medica. He set up a bio-NMR laboratory and served as the team leader, researcher, and doctoral tutor.

In this article, the researchers used multidimensional NMR technology to study the solution structure and kinetics of rabbit PrPC (91-228) and its S173N multiple point mutant proteins, and found that the rabbit PrPC protein has a unique spatial structure and dynamics. Nature of study. The researchers pointed out that the interaction of loop165-172 with the a3 helix end and the unique surface charge distribution may be the main factors leading to the unique biological and biochemical properties of the rabbit prion protein.

Researcher Lin Donghai also collaborated with the researcher of the Institute of Zoology of Kunming this year to discover a peptide molecule that can quickly clear the balance of free radicals. The related article was published in Radic. Biol. Med. The researchers used the plateau frog as a research model. The skin of the plateau frog was exposed to sunlight and strong ultraviolet rays for a long time and produced a lot of free radicals in the body. However, the level of free radicals in the plateau frog was not high. The reason is that it is born with a mechanism that can quickly scavenge free radicals.

After cooperative research, the research team discovered a new type of anti-oxidation peptide antioxidin-RL from the frog, which can quickly remove oxidative free radicals and has strong anti-oxidation effect. The NMR technique was used to analyze the solution structure of antioxidin-RL, and its interaction with oxidative free radical ABTS+ was detected. It was found that two tyrosine residues Tyr6 and Tyr12 on the peptide form a covalent bond with free radicals, and half The cystine residue Cys10 acts to rapidly scavenge free radicals.

The results of this study can help to reveal the molecular mechanism of the conformational changes of PrPC→PrPSc in prion protein and the pathogenesis of TSE. This study provides a theoretical basis for further research and development of the value of the antioxidant polypeptide antioxidin-RL in biomedical, antioxidant protection and cosmetic research and development.

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