dbacp06742
General Description
Peptide name : Aurein 1.2_mutant_R5 (R5-Aurm)
Source/Organism : Synthetic
Linear/Cyclic : Linear
Chirality : L
Sequence Information
Sequence : RRRRRGLFDIIKKIIKSF
Peptide length: 18
C-terminal modification: Linear
N-terminal modification : Free
Non-natural peptide information:
Activity Information
Assay type : MTT assay
Assay time : 24-h
Activity : 54.22% cell viability
Cell line : HT-29
Cancer type : Colon Cancer
Other activity : Antimicrobial
Physicochemical Properties
Amino acid composition bar chart :
Molecular mass : 2302.8123 Dalton
Aliphatic index : 1.083
Instability index : 124.722
Hydrophobicity (GRAVY) : -0.638
Isoelectric point : 12
Charge (pH 7) : 6.7582
Aromaticity : 11.11
Molar extinction coefficient (cysteine, cystine): (0, 0)
Hydrophobic/hydrophilic ratio : 0.8
hydrophobic moment : -0.659
Missing amino acid : A,C,E,H,M,N,P,Q,T,V,W,Y
Most occurring amino acid : R
Most occurring amino acid frequency : 5
Least occurring amino acid : G
Least occurring amino acid frequency : 1
Structural Information
3D structure :
Secondary structure fraction (Helix, Turn, Sheet): (22., 16., 38.)
SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](CC(C)C)NC(=O)CNC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@@H](N)CCCNC(=N)N)C(=O)N[C@H](C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CO)C(=O)N[C@@H](Cc1ccccc1)C(=O)O)[C@@H](C)CC)[C@@H](C)CC)[C@@H](C)CC
Secondary Structure :
| Method | Prediction |
|---|---|
| GOR | HHHHTTHHHHHHHHHHHH |
| Chou-Fasman (CF) | CCCCCCEEEEEEEEECCC |
| Neural Network (NN) | CCCCCCCCHHHHHHCCCC |
| Joint/Consensus | CCCCCCCCHHHHHHCCCC |
Molecular Descriptors and ADMET Properties
Molecular Descriptors: Click here to download
ADMET Properties: Click here to download
Cross Referencing databases
CancerPPD : Not available
ApIAPDB : Not available
CancerPPD2 ID: 7440
Reference
1 : Salarpour Garnaie H, et al. Designing Potent Anticancer Peptides by Aurein 1.2 Key Residues Mutation and Catenate Cell-Penetrating Peptide. Adv Pharm Bull. 2023; 13:583-591. doi: 10.34172/apb.2023.063
Literature
Paper title : Designing Potent Anticancer Peptides by Aurein 1.2 Key Residues Mutation and Catenate Cell-Penetrating Peptide.
Doi : https://doi.org/10.34172/apb.2023.063
Abstract : PURPOSE: Aurein 1.2 (Aur) peptide is known for possessing anticancer characteristics devoid of conventional therapeutics side effects. For improving Aur peptide anticancer functionality, different anticancer peptides were constructed based on Aur peptide through targeting two separate strategies, including (1) sequence-based mutations and (2) adding a cell-penetrating peptide linker. METHODS: The study was approached by designing three different analogs of Aur, including (a) Aur mutant (Aur<sub>m</sub>), (b) Aur with N-terminal polyarginine linker (R5-Aur), and (c) Aur<sub>m</sub> with R5 (R5-Aur<sub>m</sub>). Computational molecular dynamics simulations clearly showed higher structural stability of R5-Aur and R5-Aur<sub>m</sub> compared to Aur, solely. The α-helical properties of R5-Aur and R5-Aur<sub>m</sub> were protected during 500 ns simulations in water solution while no such structural conservation was seen for Aur in silico. RESULTS: The results of the current study highlight response to one of the main challenges of cancer therapy through selective invasion of Aur to cancer cells without significant involvement of normal cells. This issue was confirmed by different assays, including: MTT assay, flow cytometry, qPCR, and nuclei morphological observations. Furthermore, this study intensifies exploiting in silico approaches for adjusting drug delivery. The results of different assessments on designed peptides reveal an anticancer activity pattern rising from Aur toward Aur<sub>m</sub>, and R5- Aur, consecutively. CONCLUSION: The designed structure of Aur shows improved anticancer activity through molecular changes which makes it suggestable for anticancer therapies.