General Information
-
DRAMP ID
- DRAMP30318
-
Peptide Name
- Temporin L[Pro3,DLeu9,DHyp10](TL5)
-
Source
- Synthetic construct(derived from Temporin-L)
-
Family
- Coronaviridae, Herpesviridae, Paramyxoviridae
-
Gene
- Not found
-
Sequence
- FVPWFSKFlxRIL
-
Sequence Length
- 13
-
UniProt Entry
- No entry found
-
Protein Existence
- Not found
Activity Information
-
Biological Activity
- Antimicrobial, Antiviral
-
Target Organism
-
- [Ref.35216177]HSV-1:
Target Organism Activity inhibition of HSV-1 replication in Vero cells(IC50>50.00 μM,IC90>50.00 μM); - - HSV-2:
Target Organism Activity inhibition of HSV-2 replication in Vero cells(IC50>50.00 μM μM,IC90>50.00 μM); - - SARS-CoV-2:
Target Organism Activity inhibition of replication in Vero cells(IC50>50.00 μM μM,IC90>50.00 μM); - - HPIV-3: inhibition of replication in Vero cells(IC50>50.00 μM,IC90>50.00 μM);
- HCoV-229E: inhibition of replication in Vero cells(IC50>50.00 μM,IC90>50.00 μM);
- HCoV-OC43: inhibition of replication in Vero cells(IC50>50.00 μM,IC90>50.00 μM).
- [Ref.35216177]HSV-1:
-
Hemolytic Activity
-
- [Ref.35216177]<20% hemolysis against human erythrocytes at concentrations equal or above 25 μM.
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Cytotoxicity
-
- [Ref.35216177]Vero cells:CC50>100.00 μM
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Binding Target
- membrane
Structure Information
-
Linear/Cyclic
- Linear
-
N-terminal Modification
- Free
-
C-terminal Modification
- Amidation
-
Nonterminal Modifications and Unusual Amino Acids
- The 'x' at position 10 is D-hydroxyproline (Hyp).
-
Stereochemistry
- Mixed(D-Leu9,D-Hyp10)
-
Structure
- Not found
-
Structure Description
- Not found
-
Helical Wheel Diagram
-
PDB ID
- None
-
Predicted Structure
- There is no predicted structure for DRAMP30318.
Physicochemical Information
-
Formula
- C75H102N16O11
Absent Amino Acids
- ACDEGHMNQTY
Common Amino Acids
- F
Mass
- 1664.26
PI
- 11
Basic Residues
- 2
Acidic Residues
- 0
Hydrophobic Residues
- 7
Net Charge
- +2
-
Boman Index
- 128
Hydrophobicity
- 0.708
Aliphatic Index
- 82.31
Half Life
-
- Mammalian:1.1 hour
- Yeast:3 min
- E.coli:2 min
Extinction Coefficient Cystines
- 5500
Absorbance 280nm
- 458.33
Polar Residues
- 1
DRAMP30318
Comments Information
Mechanism
- TL peptides may be able to selectively induce pore formation in highly curved membrane structures (below ~250 nm in diameter), resulting in membrane lysis once a critical number of pores is formed, with the consequence of viral infectivity reduction.
Literature Information
- ·Literature 1
-
Title
- Broad-Spectrum Antiviral Activity of the Amphibian Antimicrobial Peptide Temporin L and Its Analogs.
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Pubmed ID
- 35216177
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Reference
- Int J Mol Sci. 2022 Feb 13;23(4):2060.
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Author
- Zannella C, Chianese A, Palomba L, Marcocci ME, Bellavita R, Merlino F, Grieco P, Folliero V, De Filippis A, Mangoni M, Nencioni L, Franci G, Galdiero M.
