Evidence map›Paper›PMID 38464689›Full record

ArticleRSC advances2024

Aqueous alkaline phosphate facilitates the non-exchangeable deuteration of peptides and proteins.

Tingting Zhang, Zhixiong Jin, Heng Zhao, Can Lai, Zheyi Liu, Pan Luo, Zhe Dong, Fangjun Wang

Abstract read
In one paragraph

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

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0citing papers in PubMed
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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

8 authors.

Tingting ZhangCAS Key Laboratory of Separation Sciences for Analytical Chemistry, State Key Laboratory of Molecular Reaction Dynamics, Dalian Institute of Chemical Physics, Chinese Academy of Sciences Dalian 116023 China wangfj@dicp.ac.cn.
Zhixiong JinCAS Key Laboratory of Separation Sciences for Analytical Chemistry, State Key Laboratory of Molecular Reaction Dynamics, Dalian Institute of Chemical Physics, Chinese Academy of Sciences Dalian 116023 China wangfj@dicp.ac.cn.
Heng ZhaoCAS Key Laboratory of Separation Sciences for Analytical Chemistry, State Key Laboratory of Molecular Reaction Dynamics, Dalian Institute of Chemical Physics, Chinese Academy of Sciences Dalian 116023 China wangfj@dicp.ac.cn.
Can LaiCAS Key Laboratory of Separation Sciences for Analytical Chemistry, State Key Laboratory of Molecular Reaction Dynamics, Dalian Institute of Chemical Physics, Chinese Academy of Sciences Dalian 116023 China wangfj@dicp.ac.cn.
Zheyi LiuCAS Key Laboratory of Separation Sciences for Analytical Chemistry, State Key Laboratory of Molecular Reaction Dynamics, Dalian Institute of Chemical Physics, Chinese Academy of Sciences Dalian 116023 China wangfj@dicp.ac.cn.
Pan LuoCAS Key Laboratory of Separation Sciences for Analytical Chemistry, State Key Laboratory of Molecular Reaction Dynamics, Dalian Institute of Chemical Physics, Chinese Academy of Sciences Dalian 116023 China wangfj@dicp.ac.cn.
Zhe DongShenzhen Grubbs Institute and Department of Chemistry, Guangdong Provincial Key Laboratory of Catalysis, Southern University of Science and Technology Shenzhen 518000 China.
Fangjun WangCAS Key Laboratory of Separation Sciences for Analytical Chemistry, State Key Laboratory of Molecular Reaction Dynamics, Dalian Institute of Chemical Physics, Chinese Academy of Sciences Dalian 116023 China wangfj@dicp.ac.cn.ORCID https://orcid.org/0000-0002-8118-7019

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The incorporation of deuterium into peptides and proteins holds broad applications across various fields, such as drug development and structural characterization. Nevertheless, current methods for peptide/protein deuteration often target exchangeable labile sites or require harsh conditions for stable modification. In this study, we present a late-stage approach utilizing an alkaline phosphate solution to achieve deuteration of non-exchangeable backbone sites of peptides and proteins. The specific deuteration regions are identified through ultraviolet photodissociation (UVPD) and mass spectrometry analysis. This deuteration strategy demonstrates site and structure selectivity, with a notable affinity for labeling the α-helix regions of myoglobin. The deuterium method is particularly suitable for peptides and proteins that remain stable under high pH conditions.

Identifiers

PMID38464689
PMCPMC10921277

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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.