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Sequence
- TIEEQAKTⓍLDKⓍNHEAEDLⓏYQSSLAⓍWN
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Original Sequence
- TIEEQAKTFLDKFNHEAEDLFYQSSLASWN
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Source
- Synthetic construct
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Biological Activity
- Antimicrobial, Antiviral(SARS-CoV-2)
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- Mechanism of action:The stapled peptide designed based on the ACE2 helix, which is expected to bind to SARS-CoV-2 and prevent the binding of the virus to the ACE2 receptor and disrupt the infection.
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Target Organism
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- [Ref.33310780]Virus:
- SARS-CoV-2:Inhibition of infection in HT1080/ACE2 cells(IC50=12.9 ± 0.35 μM);Inhibition of infection in A549/ACE2 cells(IC50~25 μM);
- VSV-G:Inhibition of infection in HT1080/ACE2 cells(IC50>27.6 μM);Inhibition of infection in A549/ACE2 cells(IC50>27.6 μM).
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Hemolytic Activity
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- No hemolytic activity information found.
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Cytotoxicity
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- [Ref.33310780]HT1080/ACE2 cells:CC50>27.6 μM(Less than 10% toxicity at this dose);A549/ACE2 cells:CC50>27.6 μM(Less than 10% toxicity at this dose).
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Linear/Cyclic
- Cyclic (Stapled)
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N-terminal Modification
- Acylation
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C-terminal Modification
- Amidation
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Special Amino Acid and Stapling Position
- ①The Ⓧ (position: 9,13 and 28) in sequence indicate S-2-(4'-pentenyl) alanine.②The Ⓩ (position: 21) indicates 2-(7'-octenyl) alanine in the R configuration.③ Ⓧ(9) and Ⓧ(13), Ⓩ(21) and Ⓧ(28) are cross-linked by hydrocarbon stapling.
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Secondary Structure
- 50% α-helical content in 10 mM phosphate-buffered saline (PBS)
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Structure Description
- No other descriptive information about the structure found in the literature
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There is no predicted structure for DRAMP29237.
- Literature 1
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Title
- Stapled Peptides Based on Human Angiotensin-Converting Enzyme 2 (ACE2) Potently Inhibit SARS-CoV-2 Infection In Vitro.
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Reference
- mBio. 2020 Dec 11;11(6):e02451-20.
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Author
- Curreli F, Victor SMB, Ahmed S, Drelich A, Tong X, Tseng CK, Hillyer CD, Debnath AK.