Evidence map›Paper›PMID 39609315›Full record

ArticleBiotechnology letters2024

Functional decoration of elastin-like polypeptides-based nanoparticles with a modular assembly via isopeptide bond formation.

Jun Yamaguchi, Kei Nishida, Eiry Kobatake, Masayasu Mie

Abstract read
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In one paragraph

Article in Biotechnology letters, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Jun YamaguchiDepartment of Life Science and Technology, School of Life Science and Technology, Institute of Science Tokyo, 4259 Nagatsuta-cho, Midori-ku, Yokohama, 226-8501, Japan.
Kei NishidaDepartment of Life Science and Technology, School of Life Science and Technology, Institute of Science Tokyo, 4259 Nagatsuta-cho, Midori-ku, Yokohama, 226-8501, Japan.
Eiry KobatakeDepartment of Life Science and Technology, School of Life Science and Technology, Institute of Science Tokyo, 4259 Nagatsuta-cho, Midori-ku, Yokohama, 226-8501, Japan.
Masayasu MieDepartment of Life Science and Technology, School of Life Science and Technology, Institute of Science Tokyo, 4259 Nagatsuta-cho, Midori-ku, Yokohama, 226-8501, Japan. mie.m.18e2@m.isct.ac.jp.ORCID http://orcid.org/0000-0003-2255-3346

Funding

Japan Society for the Promotion of Science 23H03738Japan Society for the Promotion of Science 23K17209
6 · The paper itself

Abstract

Temperature-responsive elastin-like polypeptides (ELPs) exhibit a low critical solution temperature-type phase transition and offer potential as useful materials for the construction of nanoparticles. Herein, we developed a novel decoration method for ELP-based nanoparticles via isopeptide bond formation with the SnoopTag/SnoopCatcher system that is not affected by the heating process required for particle formation. A mixture of a fusion protein of ELP and poly(aspartic acid) (poly(D)), known as ELP-poly(D), and ELP-poly(D) fused with SnoopCatcher (ELP-poly(D)-SnC) formed protein nanoparticles as a result of the temperature responsiveness of ELP, with the resultant nanoparticles displaying the SnoopCatcher binding domain on their surfaces. In the present study, two model proteins fused to SnoopTag were displayed on the surfaces of protein nanoparticles constructed from ELP-poly(D)-SnC and ELP-poly(D). The model proteins are enhanced green fluorescent protein (EGFP) and Renilla luciferace (Rluc), which exhibits luminescent capability and weak thermostability, respectively. EGFP on the particle surface was found to retain 48.7% activity, while Rluc exhibited almost full activity, as calculated from the binding efficiency and nanoparticle activities recovered after purification. ELP-based nanoparticles containing the SnoopTag/SnoopCatcher system offer the opportunity for particle decoration with a wide range of functional proteins via isopeptide bond formation.

Indexed as

ElastinNanoparticlesPeptidesElastin-Like PolypeptidesGreen Fluorescent ProteinsRecombinant Fusion ProteinsTemperatureElastinElastin-Like Polypeptidesenhanced green fluorescent proteinGreen Fluorescent ProteinsPeptidesRecombinant Fusion ProteinsElastin-like polypeptideIsopeptide bond formationProtein ligationProtein nanoparticlesSnoopTag/SnoopCatcher

Identifiers

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.