General Information
DRAVP ID DRAVPe00378
Peptide Name Temporin L[Pro3,DLeu9,Pro10](TL2)
Sequence FVPWFSKFlPRIL
Sequence Length 13
UniProt ID No entry found
Taxon ID None
Source Synthetic construct(derived from Temporin-L)
Validation Experimentally Validated
Origin Information
Gene Name/ID Not Available
GenBank Not Available
Amino Acid position Not Available
Domain Accession ID Not Available
Nucleotide sequence ID Not Available
Molecular Type Not Available
Chromosomal Position Not Available
Activity Information
Target Organism SARS-CoV-2,HSV,HCoV-OC43,HPIV-3,HCoV-229E
Assay
Activity
Hemolytic Activity
Cytotoxicity
Binding Target membrane
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.
Structure Information
PDB ID None
Predicted Structure Download No predicted structure available
Linear/Cyclic Linear
N-terminal Modification Free
C-terminal Modification Amidation
Other Modification None
Stereochemistry Mixed(D-Leu9)
Physicochemical Information
Formula C80H111N17O13
Absent amino acids ACDEGHMNQTY
Common amino acids F
Mass 1650.04
Pl 11
Basic residues 2
Acidic residues 0
Hydrophobic residues 7
Net charge 2
Boman Index 128
Hydrophobicity 58.46
Aliphatic Index 82.31
Half Life
Extinction Coefficient cystines 5500
Absorbance 280nm 458.33
Polar residues 1
Literature Information
Literature 1
Title Broad-Spectrum Antiviral Activity of the Amphibian Antimicrobial Peptide Temporin L and Its Analogs.
Pubmed ID 35216177
Reference Int J Mol Sci. 2022 Feb 13;23(4):2060.
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.