FEBS Journal Editor’s choice: the research article about peptide modulator of ASIC1a with a unique structure

Researchers from Laboratory of Neuroreceptors and Neuroregulators and Laboratory of Biomolecular NMR-Spectroscopy of IBCh RAS, together with the Laboratory of Biological Testing of the BIBCh, isolated and characterized Ms13-1, a new peptide of the sea anemone Metridium senile with a unique 3D-structure and a pronounced selective effect on acid-sensing ion channels ASIC1a. Ms13-1 has a spatial fold named the "Cys-ladder" by the authors, and is a member of a novel structural class. In the nanomolar range, Ms 13-1 acts as a positive allosteric modulator of ASIC1a, and the injection of the peptide into the mouse hind paw causes pain, which is suppressed by the selective antagonist of ASIC1. The work was published in the FEBS Journal and was marked as the Editors' choice for the May issue. Learn more

News

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  • Mechanism of Translation Termination Revealed science news VI.27

    Protein biosynthesis by the ribosome is one of the most important reactions in nature. The length of the polypeptide chain is strictly determined by the start and stop codons in mRNA. Translation termination is necessary for the timely completion of protein biosynthesis and the release of the polypeptide product from the ribosome. This process is regulated by specific proteins, the so-called "release factors", which recognize stop codons and mediate the hydrolysis of the ester bond in the peptidyl-tRNA molecule localized in the catalytic center of the ribosome. The new study shows the role of the release factor and the 2'-OH group of tRNA in the catalysis of polypeptide cleavage through the formation of a "bridged" cyclic intermediate. The work was published in the journal Science.

  • The molecular mechanism of redox interaction between neuroglobin and cytochrome c science news VI.12

    Neuroprotective activity of neuroglobin (Ngb) is presumably based on its redox interaction with cytochrome c (Cyt c), the mechanisms of which have not yet been elucidated. Authors developed a new methodological approach to study the electron transfer between heme proteins based on Raman spectroscopy. We studied the conformational changes in the Cyt c heme and the effect of the protein microenvironment of Cyt c and Ngb hemes on electron transfer between them using developed approach. Obtained data allowed us to propose a step-by-step mechanism of interaction between Ngb and Cyt c. Understanding the mechanisms of interaction between Ngb and Cyt c is necessary for future practical applications related to the therapy of neurodegenerative diseases.