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Piscidin 3 Cu2+
General Information
DRACP ID DRACP02086
Peptide Name Piscidin 3 Cu2+
Sequence FIHHIFRGIVHAGRSIGRFLTG
Sequence Length 22
UniProt ID Not available
PubChem CID Not available
Origin Morone saxatilis (Striped bass) (Perca saxatilis)
Type Native peptide
Classification
Active ACP
Activity Information
| Cell Line | Disease | Cancer Classified | Activity | Assay | Testing Time | Literature |
|---|---|---|---|---|---|---|
| HT-1080 | Fibrosarcoma | Sarcoma | IC50=5.52 µM | MTT/MTS assay | 24 h, 48 h | 1 |
| MDA-MB-231 | Breast adenocarcinoma | Carcinoma | IC50=5.25 µM | MTT/MTS assay | 24 h, 48 h | 1 |
| A549 | Lung adenocarcinoma | Carcinoma | IC50=2.99 µM | MTT/MTS assay | 24 h, 48 h | 1 |
| HeLa | Human papillomavirus-related endocervical adenocarcinoma | Carcinoma | IC50=1.97 µM | MTT/MTS assay | 24 h, 48 h | 1 |
Hemolytic Activity Not available
Normal (non-cancerous) Cytotoxicity Not available
Target Not available
Affinity Not available
Mechanism Metallating HDPs is an effective strategy to enhance their anticancer properties through the expansion of their mechanism of action, so that both physical and chemical damage of membranes is achieved.
Nature Anticancer; Antimicrobial; Antifungal; Antiviral; Anti-Inflammatory
Structure Information
Helicity Not available
Linear/Cyclic Linear
Disulfide/Other Bond Coordination bond: Phe1<---Cu2+--->Phe1 (Amine); Phe1<---Cu2+--->Ile2 (Amide); Phe1<---Cu2+--->His3 (Imidazole)
N-terminal Modification Free
C-terminal Modification Free
Other Modification None
Chiral L
Physicochemical Information
Formula C116H179N37O25
Absent amino acids CDEKMNPQWY
Common amino acids GI
Mass 286669
Pl 12.8
Basic residues 6
Acidic residues 0
Hydrophobic residues 10
Net charge 6
Boman Index -2156
Hydrophobicity 45.45
Aliphatic Index 106.36
Half Life
Mammalian: 1.1 hour
Yeast: 3 min
E.coli: 2 min
Extinction Coefficient cystines 0
Absorbance 280nm 0
Polar residues 6
Amino acid distribution
Literature Information
Literature 1
Pubmed ID 34135370
Title Copper-binding anticancer peptides from the piscidin family: an expanded mechanism that encompasses physical and chemical bilayer disruption
Doi 10.1038/s41598-021-91670-w
Year 2021
Literature 2
Pubmed ID 31354312
Title Substitution of lysine for isoleucine at the center of the nonpolar face of the antimicrobial peptide, piscidin-1, leads to an increase in the rapidity of bactericidal activity and a reduction in toxicity
Year 2019
Patent
Patent ID Not available
Patent Title Not available
Other Iinformation Not available
Other Published ID Not available
This work is licensed under a Creative Commons Attribution 4.0 International License.