dbacp00814
General Description
Peptide name : AAD (or Aa-Pri1)
Source/Organism : Purified from chestnut mushroom
Linear/Cyclic : Linear
Chirality : L
Sequence Information
Sequence : MDSNKDERAYAQWVIIILHNVGSSPFKIANLGLSWGKLYADGNKDKEVYPSDYNGKTVGPDEKIQINSCGRENASSGTEGSFDIVDPNDGNKTIRHFYWECPWGSKRNTWTPSGSNTKWMVEWSGQNLDSGALGTITVDVLRKGN
Peptide length: 145
C-terminal modification: Linear
N-terminal modification : Free
Non-natural peptide information: None
Activity Information
Assay type : MTT/MTS assay
Assay time : 48h
Activity : At 2.5 µM concentration,decrease in cell vibility: 35%
Cell line : HepG-2
Cancer type : Liver cancer
Other activity : Not found
Physicochemical Properties
Amino acid composition bar chart :
Molecular mass : 16103.5954 Dalton
Aliphatic index : 0.631
Instability index : 29.5952
Hydrophobicity (GRAVY) : -0.742
Isoelectric point : 5.6543
Charge (pH 7) : -2.3291
Aromaticity : 0.103
Molar extinction coefficient (cysteine, cystine): (45950, 46075)
Hydrophobic/hydrophilic ratio : 0.83544303
hydrophobic moment : -0.043
Missing amino acid : None
Most occurring amino acid : G
Most occurring amino acid frequency : 16
Least occurring amino acid : M
Least occurring amino acid frequency : 2
Structural Information
3D structure :
Secondary structure fraction (Helix, Turn, Sheet): (0.2, 0.4, 0.3)
SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@@H]1CCCN1C(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)CNC(=O)[C@@H](NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H](Cc1c[nH]c2ccccc12)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](C)NC(=O)[C@H](Cc1ccc(O)cc1)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CO)NC(=O)[C@H](CC(=O)O)NC(=O)[C@@H](N)CCSC)C(C)C)[C@@H](C)CC)[C@@H](C)CC)[C@@H](C)CC)C(C)C)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(=O)O)C(=O)NCC(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@H](C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](CC(N)=O)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@H](C(=O)N[C@H](C(=O)NCC(=O)N1CCC[C@H]1C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCCCN)C(=O)N[C@H](C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CS)C(=O)NCC(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@H](C(=O)N[C@@H](CCC(=O)O)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@@H](CC(=O)O)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(=O)O)C(=O)NCC(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCCCN)C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](Cc1c[nH]cn1)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CS)C(=O)N1CCC[C@H]1C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N[C@H](C(=O)N1CCC[C@H]1C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N[C@@H](CCSC)C(=O)N[C@H](C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@@H](CC(=O)O)C(=O)N[C@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCCCN)C(=O)NCC(=O)N[C@@H](CC(N)=O)C(=O)O)C(C)C)C(C)C)[C@@H](C)O)[C@@H](C)CC)[C@@H](C)O)C(C)C)[C@@H](C)O)[C@@H](C)O)[C@@H](C)O)[C@@H](C)CC)[C@@H](C)O)C(C)C)[C@@H](C)CC)[C@@H](C)O)[C@@H](C)CC)[C@@H](C)CC)C(C)C)[C@@H](C)O)C(C)C
Secondary Structure :
| Method | Prediction |
|---|---|
| GOR | HCTTTHHHHHHHHEEEEEECTTCCCEEEEETTCTTTEEHHTTTTTTTECCTTTTTCCCCCCCHEEEETTTCTTTTTTCCTEEEEECCTTTTTEEEEEEETCTTTTTTEEECCTTCCCEEEEEHTTCCCCTTEEEEEEEEEEHTTC |
| Chou-Fasman (CF) | CCCHHHHHHEEEEEEEEEEEECCCCHHHHHEEECCCCCCCCCHHHHEECCCCCCEEECCCCCEEEECCCCCCCCCCCCCCEEEECCCCCCEEEEEECCCCCCCCCCEEEECCCCCCCCCCCCCCCCCCCCCEEEEEEEECCCCCC |
| Neural Network (NN) | CCCCCCCHHHHHHEEEEEECCCCCCCCEHHCCHCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCEEECCCCCCCCCCCCCCCCEECCCCCCCCCEEEEECCCCCCCCCCCCCCCCCCCCEEEECCCCCCCCCCCCCEEEEEHCCCC |
| Joint/Consensus | CCCCCHHHHHHHHEEEEEECCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCEEECCCCCCCCCCCCCCEEEECCCCCCCCEEEEEECCCCCCCCCEEECCCCCCCCEEEECCCCCCCCCEEEEEEEEECCCCC |
Molecular Descriptors and ADMET Properties
Molecular Descriptors: Not available.
ADMET Properties: Not available.
Cross Referencing databases
Reference
1 : Chen Y, et al. Purification and characterization of an antitumor protein with deoxyribonuclease activity from edible mushroom Agrocybe aegerita. Mol Nutr Food Res. 2012; 56:1729-38. doi: 10.1002/mnfr.201200316
Literature
Paper title : Purification and characterization of an antitumor protein with deoxyribonuclease activity from edible mushroom Agrocybe aegerita.
Doi : https://doi.org/10.1002/mnfr.201200316
Abstract : SCOPE: Mushrooms are well known for their nutritional and medicinal value. Agrocybe aegerita has been used as a nutritious food around the world and for its herbal medicinal properties in Asia. In recent years, several antitumor proteins have been identified from A. aegerita. The objective of this study was to purify a novel antitumor protein from A. aegerita. METHODS AND RESULTS: A novel antitumor protein A. aegerita deoxyribonuclease (AAD) was purified through a two-step chromatographic procedure and was shown to possess antitumor activity against different cancer cell lines. Cells treated with AAD produced typical apoptotic morphological changes, which include chromatin condensation, the accumulation of sub-G1 cells and caspase-8 cleavage. Biochemical characterization of AAD showed that it was a member of the DNase I family and that it possessed divalent metal ion-dependent endonuclease activity. The optimal temperature for AAD activity was 50°C and its optimal pH was 8.5. The MS-identified peptides of AAD were found to match to Unigene3821, which has 97% homology with Aa-Pri1, in our A. aegerita transcriptome. CONCLUSION: We have identified a novel antitumor protein from A. aegerita. This fuller understanding of A. aegerita would help us to enhance its use in nutritional and medical applications.