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Cell-Engineered Recombinant α-Synuclein: A Gage R&R Validated Protocol

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14110%2F24%3A00139081" target="_blank" >RIV/00216224:14110/24:00139081 - isvavai.cz</a>

  • Result on the web

    <a href="https://pubs.acs.org/doi/10.1021/acs.jproteome.3c00190" target="_blank" >https://pubs.acs.org/doi/10.1021/acs.jproteome.3c00190</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1021/acs.jproteome.3c00190" target="_blank" >10.1021/acs.jproteome.3c00190</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Cell-Engineered Recombinant α-Synuclein: A Gage R&R Validated Protocol

  • Original language description

    alpha-Synuclein (alpha-Syn) misfolding and its presence in Lewy bodies are observed in almost all Parkinson's disease (PD) patients. Basic biomedical research would benefit from a quick, low-cost approach to purifying alpha-Syn and developing in vitro and in vivo models for PD. Several research groups utilize PFF-based models, yet the production of alpha-Syn PFFs is inconsistent, resulting in nonconclusive findings. Some research laboratories prepare recombinant alpha-Syn (r alpha-Syn) by molecular cloning to overexpress alpha-Syn with various purifying techniques. Laboratory-to-laboratory protocols cause considerable variability and sometimes contradictory findings. PD researchers spend more on protein than solving alpha-Syn's riddles. This article uncovered a novel method for expressing and purifying r alpha-Syn validated through gage reproducibility and repeatability (Gage R&amp;R). For the production of r alpha-Syn, we have employed the ability of a high-cell-density-based expression system to overexpress protein in BL21(DE3). A simple, high-throughput, nonchromatographical purification protocol has been devised to facilitate research with higher reproducibility, which was validated through Gage R&amp;R. A crossover experimental design was utilized, and the purified protein was characterized using orthogonal high-end analytical methods, which displayed higher similarity between the isolated r alpha-Syn. Batch-to-batch variability was the least for produced protein and hence can be utilized for exploring the iceberg of PD.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10608 - Biochemistry and molecular biology

Result continuities

  • Project

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2024

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Journal of Proteome Research

  • ISSN

    1535-3893

  • e-ISSN

    1535-3907

  • Volume of the periodical

    23

  • Issue of the periodical within the volume

    1

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    9

  • Pages from-to

    16-24

  • UT code for WoS article

    001137570700001

  • EID of the result in the Scopus database

    2-s2.0-85179151181