dbACP: A Comprehensive Database of Anti-Cancer Peptides

dbacp04593

General Description

Peptide name : Mauriporin

Source/Organism : Fat-tailed scorpion

Linear/Cyclic : Not found

Chirality : Not found

Sequence Information

Sequence : MNKKTLLVIFFITMLIVDEVNSFKIGGFIKKLWRSKLAKKLRAKGRELLKDYANRVINGGPEEEAAVPAERRR

Peptide length: 73

C-terminal modification: Not found

N-terminal modification : Not found

Non-natural peptide information: None

Activity Information

Assay type : MTT assay, Lactate dehydrogenase (LDH) Release assay

Assay time : 6h

Activity : IC50 : 27.9 μM - 283.3 μM

Cell line : SACC-83

Cancer type : Human salivary adenoid cystic carcinoma

Other activity : Not found

Physicochemical Properties

Amino acid composition bar chart :

Molecular mass : 8416.9558 Dalton

Aliphatic index : 1.028

Instability index : 48.4342

Hydrophobicity (GRAVY) : -0.256

Isoelectric point : 10.393

Charge (pH 7) : 8.5084

Aromaticity : 0.082

Molar extinction coefficient (cysteine, cystine): (6990, 6990)

Hydrophobic/hydrophilic ratio : 1.14705882

hydrophobic moment : 0.0096

Missing amino acid : C,H,Q

Most occurring amino acid : K

Most occurring amino acid frequency : 10

Least occurring amino acid : W

Least occurring amino acid frequency : 1

Structural Information

3D structure :

Secondary structure fraction (Helix, Turn, Sheet): (0.4, 0.2, 0.3)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](CO)NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CC(=O)O)NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCSC)NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](N)CCSC)[C@@H](C)O)C(C)C)[C@@H](C)CC)[C@@H](C)CC)[C@@H](C)O)[C@@H](C)CC)C(C)C)C(C)C)C(=O)NCC(=O)NCC(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@H](C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)NCC(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@@H](CC(N)=O)C(=O)NCC(=O)NCC(=O)N1CCC[C@H]1C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](C)C(=O)N[C@@H](C)C(=O)N[C@H](C(=O)N1CCC[C@H]1C(=O)N[C@@H](C)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCCNC(=N)N)C(=O)O)C(C)C)[C@@H](C)CC)C(C)C)[C@@H](C)CC

Secondary Structure :

Method Prediction
GOR HHTTHHHHEEEEEEEHHHHHHHHHHHCHHHHHHHHHHHHHHHHTHHHHHHHHTEEEETTCCHHHHHHHHHHHH
Chou-Fasman (CF) CCCCEEEEEEEEEEECCCCCCEEEEEEHHHHCCHHHHHHHHHHHHHHHHHCCCEEECCCHHHHHHHHHHHCCC
Neural Network (NN) HHCCHHHEEEEEEEEEEHCCCCCCCCCHHHHHHHHHHHHHHHHHHHHHHHCCCCCCCCCCCCCCHHHHHHHHH
Joint/Consensus CCCCCCCEEEEEEEECCCCCCCCCCCCHHHHHHHHHHHHHHHHHHHHHHHCCCEEECCCCCHHHHHHHHHHHH

Molecular Descriptors and ADMET Properties

Molecular Descriptors: Click here to download

ADMET Properties: Click here to download

Cross Referencing databases

Pubmed Id : 27207743 24184591

Uniprot : Not available

PDB : Not available

CancerPPD : Not available

ApIAPDB : Click Here

CancerPPD2 ID : Not available

Reference

1 : de Oliveira C, et al. Obesity and chronic stress are able to desynchronize the temporal pattern of serum levels of leptin and triglycerides. Peptides. 2014; 51:46-53. doi: 10.1016/j.peptides.2013.10.024

2 : Zhou XR, et al. From a pro-apoptotic peptide to a lytic peptide: One single residue mutation. Biochim Biophys Acta. 2016; 1858:1914-25. doi: 10.1016/j.bbamem.2016.05.012

Literature

Paper title : Obesity and chronic stress are able to desynchronize the temporal pattern of serum levels of leptin and triglycerides.

Doi : https://doi.org/10.1016/j.peptides.2013.10.024

Abstract : Disruption of the circadian system can lead to metabolic dysfunction as a response to environmental alterations. This study assessed the effects of the association between obesity and chronic stress on the temporal pattern of serum levels of adipogenic markers and corticosterone in rats. We evaluated weekly weight, delta weight, Lee index, and weight fractions of adipose tissue (mesenteric, MAT; subcutaneous, SAT; and pericardial, PAT) to control for hypercaloric diet-induced obesity model efficacy. Wistar rats were divided into four groups: standard chow (C), hypercaloric diet (HD), stress plus standard chow (S), and stress plus hypercaloric diet (SHD), and analyzed at three time points: ZT0, ZT12, and ZT18. Stressed animals were subjected to chronic stress for 1h per day, 5 days per week, during 80 days. The chronic exposure to a hypercaloric diet was an effective model for the induction of obesity and metabolic syndrome, increasing delta weight, Lee index, weight fractions of adipose tissue, and triglycerides and leptin levels. We confirmed the presence of a temporal pattern in the release of triglycerides, corticosterone, leptin, and adiponectin in naïve animals. Chronic stress reduced delta weight, MAT weight, and levels of triglycerides, total cholesterol, and leptin. There were interactions between chronic stress and obesity and serum total cholesterol levels, between time points and obesity and adiponectin and corticosterone levels, and between time points and chronic stress and serum leptin levels. In conclusion, both parameters were able to desynchronize the temporal pattern of leptin and triglyceride release, which could contribute to the development of metabolic diseases such as obesity and metabolic syndrome.

Paper title : From a pro-apoptotic peptide to a lytic peptide: One single residue mutation.

Doi : https://doi.org/10.1016/j.bbamem.2016.05.012

Abstract : Further discovery and design of new anticancer peptides are important for the development of anticancer therapeutics, and study on the detailed acting mechanism and structure-function relationship of peptides is critical for anticancer peptide design and application. In this study, a novel anticancer peptide ZXR-1 (FKIGGFIKKLWRSKLA) derived from a known anticancer peptide mauriporin was developed, and a mutant ZXR-2 (FKIGGFIKKLWRSLLA) with only one residue difference at the 14th position (Lys→Leu) was also engineered. Replacement of the lysine with leucine made ZXR-2 more potent than ZXR-1 in general. Even with only one residue mutation, the two peptides displayed distinct anticancer modes of action. ZXR-1 could translocate into cells, target on the mitochondria and induce cell apoptosis, while ZXR-2 directly targeted on the cell membranes and caused membrane lysis. The variance in their acting mechanisms might be due to the different amphipathicity and positive charge distribution. In addition, the two Ile-Leu pairs (3-10 and 7-14) in ZXR-2 might also play a role in improving its cytotoxicity. Further study on the structure-function relationship of the two peptides may be beneficial for the design of novel anticancer peptides and peptide based therapeutics.