Evidence map›Paper›PMID 37509158›Full record

ArticleBiomolecules2023

Design of Beta-2 Microglobulin Adsorbent Protein Nanoparticles.

Justin E Miller, Roger Castells-Graells, Mark A Arbing, Aldo Munoz, Yi-Xiao Jiang, Charlize T Espinoza, Brian Nguyen, Paul Moroz, Todd O Yeates

Open access · goldAbstract read
In one paragraph

Article in Biomolecules, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

6 citing papers in PubMed, 9 citations in OpenAlex.

  1. Review
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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

9 authors at 2 institutions in 2 countries.

Justin E MillerMolecular Biology Institute, University of California, Los Angeles, CA 90095, USA.
Roger Castells-GraellsUCLA-DOE Institute for Genomics and Proteomics, Los Angeles, CA 90095, USA.ORCID 0000-0002-3985-6194
Mark A ArbingUCLA-DOE Institute for Genomics and Proteomics, Los Angeles, CA 90095, USA.
Aldo MunozDepartment of Chemistry and Biochemistry, University of California, Los Angeles, CA 90095, USA.
Yi-Xiao JiangMolecular Biology Institute, University of California, Los Angeles, CA 90095, USA.
Charlize T EspinozaDepartment of Chemistry and Biochemistry, University of California, Los Angeles, CA 90095, USA.
Brian NguyenMolecular Biology Institute, University of California, Los Angeles, CA 90095, USA.ORCID 0000-0002-1039-6614
Paul MorozSchool of Medicine, Curtin University, Perth, WA 6845, Australia.
Todd O YeatesMolecular Biology Institute, University of California, Los Angeles, CA 90095, USA.ORCID 0000-0001-5709-9839
University of California, Los Angeles · USCurtin University · AU

Funding

Biotechnology Training in Biomedical Sciences and EngineeringT32GM067555 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI GU, ZHEN · 2005 to 2019
$2.8M
Designing Novel Protein Assemblies as Rigid Symmetric Scaffolds for Cryo-EM ImagingR01GM129854 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI YEATES, TODD O · 2019 to 2022
$1.2M
NIGMS NIH HHS R01 GM129854NIGMS NIH HHS T32 GM067555NIH HHS R01GM129854NIH HHS T32 GM067555
6 · The paper itself

Abstract

Beta-2 microglobulin (B2M) is an immune system protein that is found on the surface of all nucleated human cells. B2M is naturally shed from cell surfaces into the plasma, followed by renal excretion. In patients with impaired renal function, B2M will accumulate in organs and tissues leading to significantly reduced life expectancy and quality of life. While current hemodialysis methods have been successful in managing electrolyte as well as small and large molecule disturbances arising in chronic renal failure, they have shown only modest success in managing plasma levels of B2M and similar sized proteins, while sparing important proteins such as albumin. We describe a systematic protein design effort aimed at adding the ability to selectively remove specific, undesired waste proteins such as B2M from the plasma of chronic renal failure patients. A novel nanoparticle built using a tetrahedral protein assembly as a scaffold that presents 12 copies of a B2M-binding nanobody is described. The designed nanoparticle binds specifically to B2M through protein-protein interactions with nanomolar binding affinity (~4.2 nM). Notably, binding to the nanoparticle increases the effective size of B2M by over 50-fold, offering a potential selective avenue for separation based on size. We present data to support the potential utility of such a nanoparticle for removing B2M from plasma by either size-based filtration or by polyvalent binding to a stationary matrix under blood flow conditions. Such applications could address current shortcomings in the management of problematic mid-sized proteins in chronic renal failure patients.

Indexed as

Kidney Failure, ChronicRenal Insufficiency, Chronicbeta 2-MicroglobulinHumansNanoparticlesQuality of LifeRenal Dialysisbeta 2-Microglobulinamyloidosisbeta-2 microglobulin (B2M)dialysismiddle moleculesnanoparticlesprotein cagesprotein design

Identifiers

PMID37509158
PMCPMC10377675
OpenAlexW4384340452

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.