Evidence map›Paper›PMID 35958484›Full record

ArticleAmerican journal of translational research2022

Promoting the formation of Pi-stacking interaction to improve CTL cells activation between modified peptide and HLA.

Ying Zhu, Chang-Xin Huang, Le Zhang, Ze-Fang Wang, Dong-Li Zhao, Fei Ding, Si-Yu Zhang, Yong-Qiang Li, Ling-Zhi Chen

Abstract read
In one paragraph

Article in American journal of translational research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
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.

Ying ZhuDepartment of Oncology, The First Affiliated Hospital of Zhejiang Chinese Medical University Hangzhou 310000, Zhejiang, China.
Chang-Xin HuangDepartment of Oncology, The Affiliated Hospital of Hangzhou Normal University Hangzhou 310000, Zhejiang, China.
Le ZhangMaster Class, Zhejiang Chinese Medical University, The Fourth School of Clinical Medicine Hangzhou 310000, Zhejiang, China.
Ze-Fang WangMaster Class, Hangzhou Normal University, The School of Medicine Hangzhou 3100000, Zhejiang, China.
Dong-Li ZhaoMaster Class, Zhejiang Chinese Medical University, The Fourth School of Clinical Medicine Hangzhou 310000, Zhejiang, China.
Fei DingDepartment of Oncology, The Affiliated Hospital of Hangzhou Normal University Hangzhou 310000, Zhejiang, China.
Si-Yu ZhangDepartment of Oncology, The Affiliated Hospital of Hangzhou Normal University Hangzhou 310000, Zhejiang, China.
Yong-Qiang LiDepartment of Oncology, The Affiliated Hospital of Hangzhou Normal University Hangzhou 310000, Zhejiang, China.
Ling-Zhi ChenDepartment of Blood Transfusion, The First Hospital of Jiaxing, Affiliated Hospital of Jiaxing University Jiaxing 314000, Zhejiang, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

objectiveThis study aims to investigate the use of single residue substitution to promote the formation of pi-stacking interactions between peptides and Human leukocyte antigen (HLA)-A*2402 molecules to improve the affinity of peptides and HLA molecules, as well as the level of cytotoxic T lymphocyte (CTL) cells activated by peptides-HLA (p-HLA) complex.

methodsMolecular docking and molecular dynamics simulation were used to simulate and analyze the interactions and binding free energies between HLA-A*2402-restricted antigen peptides and HLA molecules, before and after the single residue substitution. HLA-A*2402 restricted antigen peptides before and after the single residue replacement were loaded into dendritic cells (DCs) in vitro, and further Enzyme-Linked ImmunoSpot (ELispot) test was carried out to evaluate the effect of modified antigen peptides on the immune activation of CTL cells.

resultAfter replacing the antigen peptides with a single residue, some of them could promote the formation of pi-stacking interaction. The binding free energy between the modified antigen peptides and HLA-A*2402, as well as the level of immune activation of CTL cells were mostly higher than before, especially after the replacement of the 9th residue of the polypeptide, such as C9F and C9W. There was a significant negative correlation between the level of activated CTL cells by modified antigen peptides and the total interaction amount of hydrogen bonds and salt bridges.

conclusionPromoting the formation of pi-stacking interaction between antigen peptides and HLA-A*2402 molecules could increase the total binding free energy of p-HLA complex and the level of CTL cells activation. In addition, the amount of hydrogen bonds and salt bridges between peptides and HLA could reduce the level of immune activation. All the characteristics above can improve the immunogenicities of the weak antigens.

Indexed as

molecular dynamics simulationpi-stacking (π-stacking)Residue substitutionT cell activation

Identifiers

PMID35958484
PMCPMC9360904

What OpenQuestion holds

Textmetadata
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.