Evidence map›Paper›PMID 27500277›Full record

ArticleACS sensors2016

Tuning the selectivity and sensitivity of an OmpG nanopore sensor by adjusting ligand tether length.

Monifa A Fahie, Bib Yang, Bach Pham, Min Chen

Abstract read
In one paragraph

Article in ACS sensors, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

23 citing papers in PubMed.

  1. Protein Analyte Sensing with an Outer Membrane Protein G (OmpG) Nanopore.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  2. Engineering a Monomeric Nanopore Scaffold for Multiplexed Protein Detection.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Fast slow folding of an outer membrane porin.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  9. Interplay of Affinity and Surface Tethering in Protein Recognition.The journal of physical chemistry letters · 2022
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Nanopore sensing: A physical-chemical approach.Biochimica et biophysica acta. Biomembranes · 2021
    Review
  15. Insertion state of modular protein nanopores into a membrane.Biochimica et biophysica acta. Biomembranes · 2021
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors.

Monifa A FahieMolecular and Cellular Biology Program, University of Massachusetts Amherst, Amherst, MA 01003; Department of Chemistry, University of Massachusetts Amherst, Amherst, MA 01003.
Bib YangDepartment of Chemistry, University of Massachusetts Amherst, Amherst, MA 01003.
Bach PhamDepartment of Chemistry, University of Massachusetts Amherst, Amherst, MA 01003.
Min ChenMolecular and Cellular Biology Program, University of Massachusetts Amherst, Amherst, MA 01003; Department of Chemistry, University of Massachusetts Amherst, Amherst, MA 01003.

Funding

CHEMISTRY-BIOLOGY INTERFACE PREDOCTORAL TRAINING GRANTST32GM008515 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI THOMPSON, LYNMARIE K. · 1995 to 2020
$4.3M
NIGMS NIH HHS T32 GM008515
6 · The paper itself

Abstract

We have previously shown that a biotin ligand tethered to the rim of an OmpG nanopore can be used to detect biotin-binding proteins. Here, we investigate the effect of the length of the polyethylene glycol tether on the nanopore's sensitivity and selectivity. When the tether length was increased from 2 to 45 ethylene repeats, sensitivity decreased substantially for a neutral protein streptavidin and slightly for a positively charged protein (avidin). In addition, we found that two distinct avidin binding conformations were possible when using a long tether. These conformations were sensitive to the salt concentration and applied voltage. Finally, a longer tether resulted in reduced sensitivity due to slower association for a monoclonal anti-biotin antibody. Our results highlight the importance of electrostatic, electroosmotic and electrophoretic forces on nanopore binding kinetics and sensor readout.

Indexed as

antibodybiotinnanoporeOmpGsensingstreptavidin

Identifiers

PMID27500277
PMCPMC4972499

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.