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MYP_113199
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Basic Information
Temporin-LT2 (Frogs, amphibians, animals)
Anticancer
Antimicrobial
Antimicrobial ▸ Antibacterial
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-positive
Toxicity / Safety ▸ Blood cell toxicity ▸ Hemolysis ▸ Hemolytic
Toxicity / Safety ▸ Cytolysis / cell lysis ▸ Cytolytic activity
Standard
17 amino acids
C93H153N19O19
Standard
Sequence
FLPIALKALGSIFPKIL
Physicochemical Analysis
1841.33 Da
10.00
1.76
1.55
0.1034
1.51
0.60
0.56
33.41
172.35
0.1176
0.00
0.00
The radar chart summarizes major physicochemical dimensions for quick comparison, while exact numerical values remain listed on the left.
Residue Composition
Amino Acid Composition
Chemical Descriptors
583.61
0.90
19.0
21.0
58.0
131.0
4.0
16.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0266993 VERIFIED: NO
Provenance & Taxonomy
not reported [other]
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Anticancer
PaperAntiCP 2.0: an updated model for predicting anticancer peptides (benchmark provenance; exact sequence-level experiment paper unresolved here) | https://pubmed.ncbi.nlm.nih.gov/32770192/
RECORD: Rec_0271789 VERIFIED: YES
Provenance & Taxonomy
Hylarana latouchii [Animal]
Temporin
Structure & Mods
ribosomal mature linear peptide [Linear]
Gene-encoded natural peptide composed of standard L-amino acids [L]
Amidation
Bio-Activity Profile
Antimicrobial Antibacterial Anti-Gram-positive
Staphylococcus aureus
6.8 μM
MIC
PaperH. Wang et al. / Biochimie 91 (2009) 540-547. Isolation, characterization and molecular cloning of new antimicrobial peptides belonging to the brevinin-1 and temporin families from the skin of Hylarana latouchii (Anura: Ranidae) Evidence URLhttps://www.uniprot.org/uniprotkb/C0JLF1/entry
RECORD: Rec_0314754 VERIFIED: YES
Provenance & Taxonomy
Hylarana latouchii [Animal]
Temporin
156873
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial
Staphylococcus aureus
12.5 μg/mL
MIC
PaperIsolation, characterization and molecular cloning of new antimicrobial peptides belonging to the brevinin-1 and temporin families from the skin of Hylarana latouchii (Anura: Ranidae).
RECORD: Rec_0356825 VERIFIED: YES
Provenance & Taxonomy
Hylarana latouchii [Animal]
Temporin
Structure & Mods
ribosomal mature linear peptide [Linear]
Gene-encoded natural peptide composed of standard L-amino acids [L]
Amidation
Bio-Activity Profile
Hemolytic Cytolytic
Erythrocytes
109.0 μM
HC50
PaperH. Wang et al. / Biochimie 91 (2009) 540-547. Isolation, characterization and molecular cloning of new antimicrobial peptides belonging to the brevinin-1 and temporin families from the skin of Hylarana latouchii (Anura: Ranidae) Evidence URLhttps://www.uniprot.org/uniprotkb/C0JLF1/entry
RECORD: Rec_0369504 VERIFIED: NO
Provenance & Taxonomy
Hylarana latouchii,Sylvirana latouchii [Animal]
Temporin
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Amidation
Bio-Activity Profile
Antimicrobial Antibacterial
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