Evidence map›Paper›PMID 32667815›Full record

ArticleNano letters2020

Enhancing Surface Capture and Sensing of Proteins with Low-Power Optothermal Bubbles in a Biphasic Liquid.

Youngsun Kim, Hongru Ding, Yuebing Zheng

Abstract read
In one paragraph

Article in Nano letters, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

  1. Article
  2. Article
  3. Optothermal rotation of micro-/nano-objects.Chemical communications (Cambridge, England) · 2023
    Review
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Review
  10. Heat-Mediated Optical Manipulation.Chemical reviews · 2022
    Review
  11. Article
  12. Article
  13. Liquid Optothermoelectrics: Fundamentals and Applications.Langmuir : the ACS journal of surfaces and colloids · 2021
    Article
  14. Sensitivity-Enhancing Strategies in Optical Biosensing.Small (Weinheim an der Bergstrasse, Germany) · 2021
    Review
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

3 authors.

Funding

On-Chip Multiplexed Adhesion Frequency Assay for Measuring Receptor-Ligand Interactions on CellsDP2GM128446 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI ZHENG, YUEBING · 2017 to 2017
$2.2M
NIGMS NIH HHS DP2 GM128446
6 · The paper itself

Abstract

Molecular binding in surface-based biosensing is inherently governed by diffusional transport of molecules in solution to surface-immobilized counterparts. Optothermally generated surface microbubbles can quickly accumulate solutes at the bubble-liquid-substrate interface due to high-velocity fluid flows. Despite its potential as a concentrator, however, the incorporation of bubbles into protein-based sensing is limited by high temperatures. Here, we report a biphasic liquid system, capable of generating microbubbles at a low optical power/temperature by formulating PFP as a volatile, water-immiscible component in the aqueous host. We further exploited zwitterionic surface modification to prevent unwanted printing during bubble generation. In a single protein-protein interaction model, surface binding of dispersed proteins to capture proteins was enhanced by 1 order of magnitude within 1 min by bubbles, compared to that from static incubation for 30 min. Our proof-of-concept study exploiting fluid formulation and optothermal add-on paves an effective way toward improving the performances of sensors and spectroscopies.

Indexed as

MicrobubblesDiffusionTemperaturebiphasic liquidMarangoni convectionmicrobubblesperfluorocarbonsurface-based biosensing

Identifiers

PMID32667815
PMCPMC7572762

What OpenQuestion holds

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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.