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TitleHigh-Throughput Human Histone Detection by an Engineered Actinoporin Nanopore.
Journal, issue, pagesACS Sens, Vol. 11, Issue 3, Page 2016-2029, Year 2026
Publish dateMar 27, 2026
AuthorsMarija Srnko / Gašper Šolinc / Ana Crnković / Franci Merzel / Michael Jordan / E Jayne Wallace / Marjetka Podobnik / Gregor Anderluh /
PubMed AbstractThe use of protein nanopores has proven to be very promising for the identification of proteins or the sequencing of peptides. However, their widespread use in biosensor applications is limited by ...The use of protein nanopores has proven to be very promising for the identification of proteins or the sequencing of peptides. However, their widespread use in biosensor applications is limited by more complex molecular properties of proteins in comparison to nucleic acids. Here, we developed an α-helical Fav nanopore from the coral Orbicella faveolata to detect human histones using a commercial MinION device. The engineered nanopores showed stable insertion into the polymeric membrane support. Bulk analysis of several tens to hundreds of pores per measurement revealed significant differences in mean current passing the pore and current noise resulting from capturing different full-length human histones or their post-translationally modified variants into the pore lumen. Importantly, detailed blocking analyses confirmed histone-specific signals that allow further discrimination between two medically important extracellular histones in mixtures. The newly developed Fav nanopore and high-throughput approach for the detection of biomedically important proteins is an important step towards the widespread use of nanopores in modern analytics.
External linksACS Sens / PubMed:41718555
MethodsEM (single particle)
Resolution3.05 - 3.28 Å
Structure data

50061

9eyp

EMDB-50061, PDB-9eyp:
The structure of octameric pore of RN1 variant of actinoporin Fav
Method: EM (single particle) / Resolution: 3.05 Å

50062

9eyq

EMDB-50062, PDB-9eyq:
The structure of nonameric pore of RN1 variant of actinoporin Fav
Method: EM (single particle) / Resolution: 3.28 Å

Chemicals

PDB-1h8m:
Solution structure of ykt6

Source
  • orbicella faveolata (invertebrata)
KeywordsTOXIN / Actinoporin / Pore-forming toxin / Pore / Octamer / Transmembrane pore / Protein nanopore / nonamer

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