Evidence map›Paper›PMID 36346346›Full record

ArticleACS applied materials & interfaces2022

Di-Arginine Additives for Dissociation of Gold Nanoparticle Aggregates: A Matrix-Insensitive Approach with Applications in Protease Detection.

Maurice Retout, Zhicheng Jin, Jason Tsujimoto, Yash Mantri, Raina Borum, Matthew N Creyer, Wonjun Yim, Tengyu He, Yu-Ci Chang, Jesse V Jokerst

Open access · greenAbstract read
In one paragraph

Article in ACS applied materials & interfaces, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.3field-weighted citation impact, top 22% of its field
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

12 citing papers in PubMed, 21 citations in OpenAlex.

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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

10 authors at 1 institution in 1 country.

Maurice RetoutDepartment of NanoEngineering, University of California, San Diego, La Jolla, California92093, United States.
Zhicheng JinDepartment of NanoEngineering, University of California, San Diego, La Jolla, California92093, United States.ORCID 0000-0001-6072-7533
Jason TsujimotoDepartment of Bioengineering, University of California, San Diego, La Jolla, California92093, United States.
Yash MantriDepartment of Bioengineering, University of California, San Diego, La Jolla, California92093, United States.ORCID 0000-0002-6689-2158
Raina BorumDepartment of NanoEngineering, University of California, San Diego, La Jolla, California92093, United States.ORCID 0000-0003-4265-3109
Matthew N CreyerDepartment of NanoEngineering, University of California, San Diego, La Jolla, California92093, United States.ORCID 0000-0003-1213-8245
Wonjun YimMaterials Science and Engineering Program, University of California, San Diego, La Jolla, California92093, United States.ORCID 0000-0002-0242-7898
Tengyu HeMaterials Science and Engineering Program, University of California, San Diego, La Jolla, California92093, United States.ORCID 0000-0002-6767-4849
Yu-Ci ChangMaterials Science and Engineering Program, University of California, San Diego, La Jolla, California92093, United States.ORCID 0000-0001-6997-9884
Jesse V JokerstDepartment of NanoEngineering, University of California, San Diego, La Jolla, California92093, United States.ORCID 0000-0003-2829-6408
University of California San Diego · US

Funding

A Miniaturized and High-frequency Acoustic Imaging System for Oral Health and Diseases of the Head and NeckR01DE031307 · NIDCR · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI Jesse Vincent Jokerst · 2022 to 2026
$3.1M
Validation of Smart Masks for Surveillance of COVID-19R01DE031114 · NIDCR · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI JOKERST, JESSE VINCENT · 2021 to 2023
$1.2M
Cancer Researchers in Nanotechnology (CRIN)T32CA153915 · NCI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI KUMMEL, ANDREW CLYDE, ZHANG, DONG-ER · 2017 to 2021
$994k
Non-Invasive Detection and Staging of Decubitus and Diabetic UlcersR21AG065776 · NIA · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI JOKERST, JESSE VINCENT · 2020 to 2021
$575k
Imaging SARS-CoV-2 proteases for spatio-temporal insight into Covid-19R21AI157957 · NIAID · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI JOKERST, JESSE VINCENT · 2020 to 2020
$434k
MANTA ViewSizer 3011 Nanoparticle Characterization SystemS10OD023555 · OD · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI JOKERST, JESSE VINCENT · 2018 to 2018
$137k
NCI NIH HHS T32 CA153915NIAID NIH HHS R21 AI157957NIA NIH HHS R21 AG065776NIDCR NIH HHS R01 DE031114NIDCR NIH HHS R01 DE031307NIH HHS S10 OD023555
6 · The paper itself

Abstract

We report the reversible aggregation of gold nanoparticles (AuNPs) assemblies via a di-arginine peptide additive and thiolated PEGs (HS-PEGs). The AuNPs were first aggregated by attractive forces between the citrate-capped surface and the arginine side chains. We found that the HS-PEG thiol group has a higher affinity for the AuNP surface, thus leading to redispersion and colloidal stability. In turn, there was a robust and obvious color change due to on/off plasmonic coupling. The assemblies' dissociation was directly related to the HS-PEG structural properties such as their size or charge. As an example, HS-PEGs with a molecular weight below 1 kDa could dissociate 100% of the assemblies and restore the exact optical properties of the initial AuNP suspension (prior to the assembly). Surprisingly, the dissociation capacity of HS-PEGs was not affected by the composition of the operating medium and could be performed in complex matrices such as plasma, saliva, bile, urine, cell lysates, or even seawater. The high affinity of thiols for the gold surface encompasses by far the one of endogenous molecules and is thus favored. Moreover, starting with AuNPs already aggregated ensured the absence of a background signal as the dissociation of the assemblies was far from spontaneous. Remarkably, it was possible to dry the AuNP assemblies and solubilize them back with HS-PEGs, improving the colorimetric signal generation. We used this system for protease sensing in biological fluids. Trypsin was chosen as the model enzyme, and highly positively charged peptides were conjugated to HS-PEG molecules as cleavage substrates. The increase of positive charge of the HS-PEG-peptide conjugate quenched the dissociation capacity of the HS-PEG molecules, which could only be restored by the proteolytic cleavage. Picomolar limit of detection was obtained as well as the detection in saliva or urine.

Indexed as

GoldMetal NanoparticlesArgininePeptide HydrolasesPeptidesPolyethylene GlycolsSulfhydryl CompoundsArginineGoldPeptide HydrolasesPeptidesPolyethylene GlycolsSulfhydryl Compoundscolorimetric detectiongold nanoparticlesPEGpeptidesprotease sensingreversible assembly

Identifiers

PMID36346346
PMCPMC10464667
OpenAlexW4308510857

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.