repository
Structurally constrained peptides prevent SARS-CoV-2 spike – hACE2 interaction and neutralize pseudovirus in vitro.
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.advisor | Woo Hyun Goo | - |
| dc.contributor.author | TRINH THANH THAO | - |
| dc.date.accessioned | 2025-01-25T01:35:52Z | - |
| dc.date.available | 2025-01-25T01:35:52Z | - |
| dc.date.issued | 2023-08 | - |
| dc.identifier.other | 33107 | - |
| dc.identifier.uri | https://dspace.ajou.ac.kr/handle/2018.oak/24305 | - |
| dc.description | 학위논문(석사)--아주대학교 일반대학원 :의생명과학과,2023. 8 | - |
| dc.description.tableofcontents | BACKGROUND 1 <br> 1. The pandemic 1 <br> 2. SARS-CoV-2 1 <br> a. Biology of SARS-CoV-2 1 <br> b. Cell entry of SARS-CoV-2 2 <br> c. Evolution of SARS-CoV-2 and Spike mutation 4 <br> 3. SARS-CoV-2 spike neutralization. 5 <br>MATERIALS AND METHODS 7 <br> Neutralizing peptides designing process and synthesis. 7 <br> Surface plasmon resonance (SPR) analysis 7 <br> Cell culturing 7 <br> Transient transfection 8 <br> Pseudovirus particles production 8 <br> Fluorescence microscope 9 <br> qPCR 9 <br> Pseudovirus-based neutralizing assay (Luciferase assay) 10 <br> Cell viability assay 10 <br> Proteinase K assay 10 <br>RESULTS 12 <br> 1. Candidates for neutralizing peptides 12 <br> 2. The neutralizing peptides are not toxic to the cells. 15 <br> 3. Human ACE2 expressing cell line construction. 16 <br> 4. Neutralize effects of peptides on different variants 18 <br> 5. The peptides work in dose-dependent manners. 20 <br> 6. Stability of neutralizing peptides 22 <br>DISCUSSION 23 <br>CONCLUSION 25 <br>REFERENCES 26 | - |
| dc.language.iso | eng | - |
| dc.publisher | The Graduate School, Ajou University | - |
| dc.rights | 아주대학교 논문은 저작권에 의해 보호받습니다. | - |
| dc.title | Structurally constrained peptides prevent SARS-CoV-2 spike – hACE2 interaction and neutralize pseudovirus in vitro. | - |
| dc.type | Thesis | - |
| dc.contributor.affiliation | 아주대학교 대학원 | - |
| dc.contributor.department | 일반대학원 의생명과학과 | - |
| dc.date.awarded | 2023-08 | - |
| dc.description.degree | Master | - |
| dc.identifier.localId | T000000033107 | - |
| dc.identifier.url | https://dcoll.ajou.ac.kr/dcollection/common/orgView/000000033107 | - |
| dc.subject.keyword | SARS-CoV-2 | - |
| dc.description.alternativeAbstract | COVID-19 became a worldwide pandemic shortly after the first emergence of SARS-CoV-2 in December 2019. The virus possesses a high dynamic of evolution, with several mutations have been occurred and many variations of concern (VOCs). The infection is initiated by the interaction of SARS-CoV-2 receptor binding domain (RBD) and hACE2. ACE2 converts angiotensin I to angiotensin 1-9, and hACE2 is the receptor for the spike of SARS-CoV-2. The RBD is immunodominant, this region is the target of vaccine, antibodies, and peptides design. RBD is the poorly conserved region of S protein, the mutations in RBD resulted in many immune escapes, and the approved antibodies lost their susceptibility. In this study, the neutralizing effect of neutralizing peptides CSNP1, CSNP4 and Pep1 was measured in vitro, using the model of HEK293 cells that highly expresses hACE2 as the host cell, and lentiviruses that carry the SARS- CoV-2 spike proteins on their surface as the pseudovirus particles. The results showed that all CSNP1, CSNP4 and Pep1 strongly inhibit the infection of SARS- CoV-2 and have neutralizing effects on all VOCs. The peptides work in dose- dependent manner and do show cytotoxicity even in high concentrations. Taken together, neutralizing peptides based of the structure of hACE2 universally deter the SARS-CoV-2 infections, and the three neutralizing peptides CSNP1, CSNP4, and pep1 are promising candidates in treatment of the new emerging SARS-CoV-2 variants and ready to go in clinical tests. | - |
- Appears in Collections:
- Graduate School of Ajou University > Department of Biomedical Sciences > 3. Theses(Master)
- Files in This Item:
- There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.
-
- License
- STATISTICS
- Total Visit :5,245,118
- Total Download :2,137
- Today View :12,955
