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Original Sequence
- IDWKKLLDAAKQIL
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Source
- Synthetic construct
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Biological Activity
- Antimicrobial, Antibacterial, Anti-Gram+
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- Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.
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Target Organism
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- [Ref.29075946] Gram-positive bacteria: Bacillus subtilis (MIC = 1.6 μg/mL), Staphylococcus aureus (MIC = 2.4 μg/mL), Staphylococcus epidermidis (MIC > 100 μg/mL);
- Gram-negative bacteria: Escherichia coli (MIC > 100 μg/mL), Shigella dysenteriae (MIC > 100 μg/mL), Salmonella typhimurium (MIC > 100 μg/mL), Klebsiella pneumoniae (MIC > 100 μg/mL), Pseudomonas aeruginosa (MIC > 100 μg/mL)
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Hemolytic Activity
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- [Ref.29075946] It has 6.7% hemolysis against human red blood cells at 12.5 μM and 12.3% hemolysis at 25 μM.
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Cytotoxicity
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No cytotoxicity information found in the reference(s) presented
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Linear/Cyclic
- Cyclic (Stapled)
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N-terminal Modification
- Free
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C-terminal Modification
- Amidation
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Special Amino Acid and Stapling Position
- ①The Ⓧ (position: 6 and 10) in sequence indicates (S)-α-methyl, α-pentenylglycine. ②Ⓧ (6) and Ⓧ (10) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.
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Secondary Structure
- 96.1% α-helical content in a 25 mM potassium phosphate buffer solution at 20℃
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Structure Description
- ①Helical contents of all stapled analogues were increased by more than a three-fold compared to their unmodified counterpart, MP1. ②MP1S appears to be the most helical among this panel of peptides, showing 96% helicity, which is 3.7-fold higher than that of MP1.
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- Literature 1
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Title
- Antimicrobial activity and stability of stapled helices of polybia-MP1
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Reference
- Arch Pharm Res. 2017 Dec;40(12):1414-1419. doi: 10.1007/s12272-017-0963-5. Epub 2017 Oct 26.
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Author
- Huy X Luong, Do-Hee Kim, Bong-Jin Lee, Young-Woo Kim