All

What are you looking for?

All
Projects
Results
Organizations

Quick search

  • Projects supported by TA ČR
  • Excellent projects
  • Projects with the highest public support
  • Current projects

Smart search

  • That is how I find a specific +word
  • That is how I leave the -word out of the results
  • “That is how I can find the whole phrase”

Assessing the impact of His-tags on activity and stability of staphylokinase variants

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00159816%3A_____%2F25%3A00082379" target="_blank" >RIV/00159816:_____/25:00082379 - isvavai.cz</a>

  • Alternative codes found

    RIV/00216224:14310/25:00142671

  • Result on the web

    <a href="https://www.sciencedirect.com/science/article/pii/S0141813025082121" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0141813025082121</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.ijbiomac.2025.147655" target="_blank" >10.1016/j.ijbiomac.2025.147655</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Assessing the impact of His-tags on activity and stability of staphylokinase variants

  • Original language description

    Staphylokinase (SAK), a potent plasminogen activator, is a promising thrombolytic agent, but its clinical application is limited by immunogenicity and stability concerns. In addition to intrinsic sequence variants, recombinant protein production often introduces affinity tags, such as the N-terminal polyhistidine (His-tag), whose potential effects on protein&apos;s biophysical and functional properties remain poorly understood. Here, we systematically investigated the impact of His-tagging on the stability and activity of four SAK variants: wild-type and non-immunogenic (triple-alanine, 3A) forms of two naturally occurring SAK types, SAK STAR and SAK 42D. Thermal and pH stability were assessed using circular dichroism and tryptophan fluorescence spectroscopy, and plasminogen-activating efficiency was evaluated through chromogenic assays. We found that while the His-tag had little effect on thermal stability and only modestly influenced functional activity, it significantly destabilized SAK under acidic conditions, and altered unfolding transitions, indicating the presence of intermediate conformations. Among the tested proteins, SAK STAR demonstrated the best structural and functional robustness, whereas SAK 42D 3A was the least stable and most prone to aggregation. These results highlight the need to assess the biophysical effect of affinity tags and point SAK STAR as the most suitable candidate for next therapeutic development.

  • 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

    <a href="/en/project/LX22NPO5107" target="_blank" >LX22NPO5107: National institute for Neurological Research</a><br>

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Others

  • Publication year

    2025

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    International Journal of Biological Macromolecules

  • ISSN

    0141-8130

  • e-ISSN

    1879-0003

  • Volume of the periodical

    328

  • Issue of the periodical within the volume

    Nov 2025

  • Country of publishing house

    NL - THE KINGDOM OF THE NETHERLANDS

  • Number of pages

    10

  • Pages from-to

    147655

  • UT code for WoS article

    001576696500001

  • EID of the result in the Scopus database