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[F30A]cHLH-p53-R
General Information
DRACP ID DRACP02846
Peptide Name [F30A]cHLH-p53-R
Sequence GARELRRLERELRRLEGGGGGGGKLAALKAKLLWLKLAC
Sequence Length 39
UniProt ID Not available
PubChem CID Not available
Origin Synthetic
Type Synthetic peptide
Classification
Active ACP Membrane lysis Cell-penetrating peptides
Activity Information
| Cell Line | Disease | Cancer Classified | Activity | Assay | Testing Time | Literature |
|---|---|---|---|---|---|---|
| MM96L | Melanoma | Carcinoma | CC50>64 μM | Resazurin assay | 26 h | 1 |
| MDA-MB-435S | Amelanotic melanoma | Carcinoma | CC50>32 μM | Resazurin assay | 26 h | 1 |
| MCF-7 | Invasive breast carcinoma of no special type | Carcinoma | CC50>64 μM | Resazurin assay | 26 h | 1 |
| MDA-MB-231 | Breast adenocarcinoma | Carcinoma | CC50>64 μM | Resazurin assay | 26 h | 1 |
| K562 | Blast phase chronic myelogenous leukemia, BCR-ABL1 positive; Chronic myeloid leukemia | Leukemia | CC50=36.7 ± 1.9 μM | Resazurin assay | 26 h | 1 |
Hemolytic Activity Human erythrocytes: 50% Hemolysis>64 µM
Normal (non-cancerous) Cytotoxicity HFF-1: CC50>64 µM; MCF-10A: CC50>64 µM; Human PBMC: CC50>64 µM
Target Not available
Affinity Not available
Mechanism (1) The positively charged peptide targets the negative surface of cancer cells via electrostatic attractions; (2) The peptide inserts into cell membranes and enters inside cells very efficaciously; (3) Once inside cells, the peptide induces toxicity through fusion and/or disruption of intracellular organelles; (4) The cell membrane is disrupted and the cells die.
Nature Anticancer
Structure Information
Helicity Not available
Linear/Cyclic Cyclic
Disulfide/Other Bond TIE: N-terminal Chloroacetic acid<--->Cys39
N-terminal Modification CAA, Chloroacetic acid
C-terminal Modification Free
Other Modification None
Chiral L
Physicochemical Information
Formula C185H324N62O48S
Absent amino acids DFHIMNPQSTVY
Common amino acids L
Mass 489507
Pl 11.55
Basic residues 10
Acidic residues 4
Hydrophobic residues 16
Net charge 6
Boman Index -6958
Hydrophobicity -28.72
Aliphatic Index 112.82
Half Life
Mammalian: 30 hour
Yeast: >20 hour
E.coli: >10 hour
Extinction Coefficient cystines 5500
Absorbance 280nm 144.74
Polar residues 9
Amino acid distribution
Literature Information
Literature 1
Pubmed ID 31390185
Title Cell Membrane Composition Drives Selectivity and Toxicity of Designed Cyclic Helix-Loop-Helix Peptides with Cell Penetrating and Tumor Suppressor Properties
Doi 10.1021/acschembio.9b00593
Year 2019
Patent
Patent ID Not available
Patent Title Not available
Other Iinformation Not available
Other Published ID Not available
External Code
DBAASP ID DBAASPS_17186
This work is licensed under a Creative Commons Attribution 4.0 International License.