Evidence map›Paper›PMID 37885585›Full record

ArticleJACS Au2023

DNA Framework Programmed Conformational Reconstruction of Antibody Complementary Determining Region.

Liqi Zhou, Lei Ren, Zhiang Bai, Qinglin Xia, Yue Wang, Hongzhen Peng, Qinglong Yan, Jiye Shi, Bin Li, Linjie Guo and 1 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in JACS Au, 2023. 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

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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

11 authors.

Liqi ZhouNational Laboratory of Solid State Microstructures, Jiangsu Key Laboratory of Artificial Functional Materials, College of Engineering and Applied Sciences and Collaborative Innovation Center of Advanced Microstructures, Nanjing University, Nanjing 210093, People's Republic of China.
Lei RenInstitute of Materiobiology, College of Science, Shanghai University, Shanghai 200444, People's Republic of China.
Zhiang BaiInstitute of Materiobiology, College of Science, Shanghai University, Shanghai 200444, People's Republic of China.
Qinglin XiaInstitute of Materiobiology, College of Science, Shanghai University, Shanghai 200444, People's Republic of China.
Yue WangInstitute of Materiobiology, College of Science, Shanghai University, Shanghai 200444, People's Republic of China.
Hongzhen PengInstitute of Materiobiology, College of Science, Shanghai University, Shanghai 200444, People's Republic of China.
Qinglong YanXiangfu Laboratory, Jiashan 314102, People's Republic of China.
Jiye ShiCAS Key Laboratory of Interfacial Physics and Technology, Shanghai Institute of Applied Physics, Chinese Academy of Sciences, Shanghai 201800, People's Republic of China.
Bin LiCAS Key Laboratory of Interfacial Physics and Technology, Shanghai Institute of Applied Physics, Chinese Academy of Sciences, Shanghai 201800, People's Republic of China.
Linjie GuoInstitute of Materiobiology, College of Science, Shanghai University, Shanghai 200444, People's Republic of China.
Lihua WangInstitute of Materiobiology, College of Science, Shanghai University, Shanghai 200444, People's Republic of China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The conformation of complementary determining region (CDR) is crucial in dictating its specificity and affinity for binding with an antigen, making it a focal point in artificial antibody engineering. Although desirable, programmable scaffolds that can regulate the conformation of individual CDRs with nanometer precision are still lacking. Here, we devise a strategy to program the CDR conformation by anchoring both ends of a free CDR loop to specific sites of a DNA framework structure. This method allows us to define the span of a single CDR loop with an ∼2 nm resolution. Using this approach, we create a series of DNA framework based artificial antibodies (DNFbodies) with varied CDR loop spans, leading to different antibody-antigen binding affinities. We find that an optimized single CDR loop (∼2.3 nm span) exhibits ∼3-fold improved affinity relative to natural antibodies, confirming the critical role of the CDR conformation. This study may inspire the rational design of artificial antibodies.

Identifiers

PMID37885585
PMCPMC10598557

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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.