Evidence map›Paper›PMID 31789500›Full record

ArticleACS nano2020

Discovery of Stable and Selective Antibody Mimetics from Combinatorial Libraries of Polyvalent, Loop-Functionalized Peptoid Nanosheets.

Jae Hong Kim, Samuel C Kim, Mark A Kline, Elissa M Grzincic, Blakely W Tresca, Joshua Cardiel, Mohsen Karbaschi, Dilani C Dehigaspitiya, Yulin Chen, Venkatareddy Udumula and 10 more

Open access · greenAbstract read
In one paragraph

Article in ACS nano, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

18 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
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  3. Polymorphism in Self-Assembly of Short Peptoid Sequences.Polymer science & technology (Washington, D.C.) · 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

20 authors at 4 institutions in 1 country.

Jae Hong KimThe Molecular Foundry , Lawrence Berkeley National Laboratory , Berkeley , California 94720 , United States.
Samuel C KimDepartment of Bioengineering and Therapeutic Sciences , University of California, San Francisco , San Francisco , California 94158 , United States.ORCID 0000-0001-5237-6358
Mark A KlineThe Molecular Foundry , Lawrence Berkeley National Laboratory , Berkeley , California 94720 , United States.
Elissa M GrzincicThe Molecular Foundry , Lawrence Berkeley National Laboratory , Berkeley , California 94720 , United States.
Blakely W TrescaThe Molecular Foundry , Lawrence Berkeley National Laboratory , Berkeley , California 94720 , United States.
Joshua CardielDepartment of Bioengineering and Therapeutic Sciences , University of California, San Francisco , San Francisco , California 94158 , United States.
Mohsen KarbaschiDepartment of Bioengineering and Therapeutic Sciences , University of California, San Francisco , San Francisco , California 94158 , United States.
Dilani C DehigaspitiyaDepartment of Chemistry , New York University , New York , New York 10003 , United States.
Yulin ChenPhysical Sciences Division , Pacific Northwest National Laboratory , Richland , Washington 99352 , United States.
Venkatareddy UdumulaPhysical Sciences Division , Pacific Northwest National Laboratory , Richland , Washington 99352 , United States.
Tengyue JianPhysical Sciences Division , Pacific Northwest National Laboratory , Richland , Washington 99352 , United States.ORCID 0000-0002-4463-5492
Daniel J MurrayThe Molecular Foundry , Lawrence Berkeley National Laboratory , Berkeley , California 94720 , United States.
Lisa YunThe Molecular Foundry , Lawrence Berkeley National Laboratory , Berkeley , California 94720 , United States.ORCID 0000-0001-7940-4902
Michael D ConnollyThe Molecular Foundry , Lawrence Berkeley National Laboratory , Berkeley , California 94720 , United States.
Jianfang LiuThe Molecular Foundry , Lawrence Berkeley National Laboratory , Berkeley , California 94720 , United States.
Gang RenThe Molecular Foundry , Lawrence Berkeley National Laboratory , Berkeley , California 94720 , United States.ORCID 0000-0002-8036-2321
Chun-Long ChenPhysical Sciences Division , Pacific Northwest National Laboratory , Richland , Washington 99352 , United States.ORCID 0000-0002-5584-824X
Kent KirshenbaumDepartment of Chemistry , New York University , New York , New York 10003 , United States.
Adam R AbateDepartment of Bioengineering and Therapeutic Sciences , University of California, San Francisco , San Francisco , California 94158 , United States.ORCID 0000-0001-9614-4831
Ronald N ZuckermannThe Molecular Foundry , Lawrence Berkeley National Laboratory , Berkeley , California 94720 , United States.ORCID 0000-0002-3055-8860
Lawrence Berkeley National Laboratory · USPacific Northwest National Laboratory · USUniversity of California, San Francisco · USNew York University · US

Funding

Structure-Function Relationship Studies of the Plasma Lipid Transfer Proteins CETP and PLTPR01HL115153 · NHLBI · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI REN, GANG · 2012 to 2021
$3.9M
Lipoprotein Structure and Function by Individual Particle Electron TomographyR01GM104427 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI REN, GANG · 2013 to 2016
$1.3M
NHLBI NIH HHS R01 HL115153NIGMS NIH HHS R01 GM104427
6 · The paper itself

Abstract

The ability of antibodies to bind a wide variety of analytes with high specificity and high affinity makes them ideal candidates for therapeutic and diagnostic applications. However, the poor stability and high production cost of antibodies have prompted exploration of a variety of synthetic materials capable of specific molecular recognition. Unfortunately, it remains a fundamental challenge to create a chemically diverse population of protein-like, folded synthetic nanostructures with defined molecular conformations in water. Here we report the synthesis and screening of combinatorial libraries of sequence-defined peptoid polymers engineered to fold into ordered, supramolecular nanosheets displaying a high spatial density of diverse, conformationally constrained peptoid loops on their surface. These polyvalent, loop-functionalized nanosheets were screened using a homogeneous Förster resonance energy transfer (FRET) assay for binding to a variety of protein targets. Peptoid sequences were identified that bound to the heptameric protein, anthrax protective antigen, with high avidity and selectivity. These nanosheets were shown to be resistant to proteolytic degradation, and the binding was shown to be dependent on the loop display density. This work demonstrates that key aspects of antibody structure and function-the creation of multivalent, combinatorial chemical diversity within a well-defined folded structure-can be realized with completely synthetic materials. This approach enables the rapid discovery of biomimetic affinity reagents that combine the durability of synthetic materials with the specificity of biomolecular materials.

Indexed as

Combinatorial Chemistry TechniquesDrug DiscoveryAntibodiesFluorescence Resonance Energy TransferMolecular StructureNanostructuresParticle SizePeptoidsProtein EngineeringSurface PropertiesAntibodiesPeptoidsbioinspired polymerscombinatorial displaymultivalent molecular recognitionprotein-mimetic materialstwo-dimensional nanomaterials

Identifiers

PMID31789500
PMCPMC9506602
OpenAlexW2989720376

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.