Evidence map›Paper›PMID 29351815›Full record

ArticleJournal of nanobiotechnology2018

Ready-to-use protein G-conjugated gold nanorods for biosensing and biomedical applications.

S Centi, F Ratto, F Tatini, S Lai, R Pini

Open access · goldAbstract read
In one paragraph

Article in Journal of nanobiotechnology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

5 citing papers in PubMed, 25 citations in OpenAlex.

  1. SERSµDrop: A Platform to Study Cell-Cell Communication via SERS Imaging.Small (Weinheim an der Bergstrasse, Germany) · 2026
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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

5 authors at 1 institution in 1 country.

S CentiInstitute of Applied Physics, National Research Council of Italy, Via Madonna del Piano, 10, 50019, Sesto Fiorentino, Italy. s.centi@ifac.cnr.it.ORCID http://orcid.org/0000-0001-5432-5589
F RattoInstitute of Applied Physics, National Research Council of Italy, Via Madonna del Piano, 10, 50019, Sesto Fiorentino, Italy.
F TatiniInstitute of Applied Physics, National Research Council of Italy, Via Madonna del Piano, 10, 50019, Sesto Fiorentino, Italy.
S LaiInstitute of Applied Physics, National Research Council of Italy, Via Madonna del Piano, 10, 50019, Sesto Fiorentino, Italy.
R PiniInstitute of Applied Physics, National Research Council of Italy, Via Madonna del Piano, 10, 50019, Sesto Fiorentino, Italy.
National Research Council · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundGold nanorods (GNRs) display unique capacity to absorb and scatter near infrared light, which arises from their peculiar composition of surface plasmon resonances. For this reason, GNRs have become an innovative material of great hope in nanomedicine, in particular for imaging and therapy of cancer, as well as in photonic sensing of biological agents and toxic compounds for e.g. biomedical diagnostics, forensic analysis and environmental monitoring. As the use of GNRs is becoming more and more popular, in all these contexts, there is emerging a latent need for simple and versatile protocols for their modification with targeting units that may convey high specificity for any analyte of interest of an end-user.

resultsWe introduce protein G-coated GNRs as a versatile solution for the oriented immobilization of antibodies in a single step of mixing. We assess this strategy against more standard covalent binding of antibodies, in terms of biocompatibility and efficiency of molecular recognition in buffer, serum and plasma, in the context of the development of a direct immunoenzymatic assay. In both cases, we estimate an average of around 30 events of molecular recognition per particle. In addition, we disclose a convenient protocol to store these particles for months in a freezer, without any detrimental effect.

conclusionsThe biocompatibility and efficiency of molecular recognition is similar in either case of GNRs that are modified with antibodies by covalent binding or oriented immobilization through protein G. However, protein G-coated GNRs are most attractive for an end-user, owing to their unique versatility and ease of bioconjugation with antibodies of her/his choice.

Indexed as

AnimalsBacterial ProteinsBiomedical TechnologyBiosensing TechniquesCell DeathGoldHeLa CellsHumansImmobilized ProteinsImmunoassayKineticsMiceNanotubesBacterial ProteinsGoldIgG Fc-binding protein, StreptococcusImmobilized ProteinsAntibody-antigen recognitionGold nanorodsPlasmaProtein GSerumStorage

Identifiers

PMID29351815
PMCPMC5775603
OpenAlexW2791987730

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.