Evidence map›Paper›PMID 38435828›Full record

ArticleBioengineering & translational medicine2024

A bioengineered anti-VEGF protein with high affinity and high concentration for intravitreal treatment of wet age-related macular degeneration.

Chengnan Huang, Yuelin Wang, Jinliang Huang, Huiqin Liu, Zhidong Chen, Yang Jiang, Youxin Chen, Feng Qian

Abstract read
In one paragraph

Article in Bioengineering & translational medicine, 2024. 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
–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

6 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
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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

8 authors.

Chengnan HuangSchool of Pharmaceutical Sciences, Beijing Frontier Research Center for Biological Structure, and Key Laboratory of Bioorganic Phosphorus Chemistry & Chemical Biology (Ministry of Education) Tsinghua University Beijing People's Republic of China.ORCID https://orcid.org/0000-0002-3313-8634
Yuelin WangDepartment of Ophthalmology Peking Union Medical College Hospital, Peking Union Medical College, Chinese Academy of Medical Sciences Beijing People's Republic of China.
Jinliang HuangQuaerite Biopharm Research Beijing People's Republic of China.
Huiqin LiuQuaerite Biopharm Research Beijing People's Republic of China.
Zhidong ChenSchool of Pharmaceutical Sciences, Beijing Frontier Research Center for Biological Structure, and Key Laboratory of Bioorganic Phosphorus Chemistry & Chemical Biology (Ministry of Education) Tsinghua University Beijing People's Republic of China.
Yang JiangDepartment of Ophthalmology Peking Union Medical College Hospital, Peking Union Medical College, Chinese Academy of Medical Sciences Beijing People's Republic of China.
Youxin ChenDepartment of Ophthalmology Peking Union Medical College Hospital, Peking Union Medical College, Chinese Academy of Medical Sciences Beijing People's Republic of China.
Feng QianSchool of Pharmaceutical Sciences, Beijing Frontier Research Center for Biological Structure, and Key Laboratory of Bioorganic Phosphorus Chemistry & Chemical Biology (Ministry of Education) Tsinghua University Beijing People's Republic of China.ORCID https://orcid.org/0000-0001-7415-6997

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Intravitreal (IVT) injection of anti-vascular endothelial growth factor (anti-VEGF) has greatly improved the treatment of many retinal disorders, including wet age-related macular degeneration (wAMD), which is the third leading cause of blindness. However, frequent injections can be difficult for patients and may lead to various risks such as elevated intraocular pressure, infection, and retinal detachment. To address this issue, researchers have found that IVT injection of anti-VEGF proteins at their maximally viable concentration and dose can be an effective strategy. However, the intrinsic protein structure can limit the maximum concentration due to stability and solution viscosity. To overcome this challenge, we developed a novel anti-VEGF protein called nanoFc by fusing anti-VEGF nanobodies with a crystallizable fragment (Fc). NanoFc has demonstrated high binding affinity to VEGF

Indexed as

high concentration proteinintravitreal injectionmultivalencynanobodyprotein engineering

Identifiers

PMID38435828
PMCPMC10905556

What Socratic 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 Socratic graph.