Peptide name : Antimicrobial peptide TsAP-1

Source/Organism : Brazilian scorpion

Linear/Cyclic : Linear

Chirality : Not found

Peptide length: 73

C-terminal modification: Linear

N-terminal modification : Amidation

Non-natural peptide information: None

Assay type : MTT Cell viability assay

Assay time : 24h

Activity : IC50 : 0.83 - 2.0 μM

Cell line : PC-3

Cancer type : androgen-independent Prostate adenocarcinoma

Other activity : Hemolytic activity

Amino acid composition bar chart :

Molecular mass : 8409.8422 Dalton

Aliphatic index : 1.202

Instability index : 43.6466

Hydrophobicity (GRAVY) : 0.1301

Isoelectric point : 7.8948

Charge (pH 7) : 0.5908

Aromaticity : 0.082

Molar extinction coefficient (cysteine, cystine): (2980, 2980)

Hydrophobic/hydrophilic ratio : 1.14705882

hydrophobic moment : -0.236

Missing amino acid : N,W

Most occurring amino acid : L

Most occurring amino acid frequency : 12

Least occurring amino acid : H

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.4, 0.1, 0.4)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](CO)NC(=O)CNC(=O)CNC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC(=O)[C@@H]1CCCN1C(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CS)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](C)NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](N)CCSC)[C@@H](C)CC)[C@@H](C)CC)[C@@H](C)O)C(C)C)[C@@H](C)CC)C(C)C)[C@@H](C)CC)C(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H](C)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](CCCCN)C(=O)NCC(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@H](C(=O)N[C@@H](CO)C(=O)N[C@@H](C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](C)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(=O)O)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](CC(=O)O)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CC(C)C)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCSC)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)O)[C@@H](C)CC)[C@@H](C)CC

1 : Guo X, et al. Two peptides, TsAP-1 and TsAP-2, from the venom of the Brazilian yellow scorpion, Tityus serrulatus: evaluation of their antimicrobial and anticancer activities. Biochimie. 2013; 95:1784-94. doi: 10.1016/j.biochi.2013.06.003

2 : Ruchala M, et al. Individual plasma ghrelin changes in the same patients in hyperthyroid, hypothyroid and euthyroid state. Peptides. 2014; 51:31-4. doi: 10.1016/j.peptides.2013.10.018

Paper title : Two peptides, TsAP-1 and TsAP-2, from the venom of the Brazilian yellow scorpion, Tityus serrulatus: evaluation of their antimicrobial and anticancer activities.

Doi : https://doi.org/10.1016/j.biochi.2013.06.003

Abstract : Here we report two novel 17-mer amidated linear peptides (TsAP-1 and TsAP-2) whose structures were deduced from cDNAs cloned from a venom-derived cDNA library of the Brazilian yellow scorpion, Tityus serrulatus. Both mature peptides were structurally-characterised following their location in chromatographic fractions of venom and synthetic replicates of each were subjected to a range of biological assays. The peptides were each active against model test micro-organisms but with different potencies. TsAP-1 was of low potency against all three test organisms (MICs 120-160 μM), whereas TsAP-2 was of high potency against the Gram-positive bacterium, Staphylococcus aureus (MIC 5 μM) and the yeast, Candida albicans (10 μM). Haemolytic activity of TsAP-1 was low (4% at 160 μM) and in contrast, that of TsAP-2 was considerably higher (18% at 20 μM). Substitution of four neutral amino acid residues with Lys residues in each peptide had dramatic effects on their antimicrobial potencies and haemolytic activities, particularly those of TsAP-1. The MICs of the enhanced cationic analogue (TsAP-S1) were 2.5 μM for S. aureus/C. albicans and 5 μM for E. coli but with an associated large increase in haemolytic activity (30% at 5 μM). The same Lys residue substitutions in TsAP-2 produced a dramatic effect on its MIC for E. coli lowering this from >320 μM to 5 μM. TsAP-1 was ineffective against three of the five human cancer cell lines tested while TsAP-2 inhibited the growth of all five. Lys residue substitution of both peptides enhanced their potency against all five cell lines with TsAp-S2 being the most potent with IC50 values ranging between 0.83 and 2.0 μM. TsAP-1 and TsAP-2 are novel scorpion venom peptides with broad spectrum antimicrobial and anticancer cell activities the potencies of which can be significantly enhanced by increasing their cationicity.

Paper title : Individual plasma ghrelin changes in the same patients in hyperthyroid, hypothyroid and euthyroid state.

Doi : https://doi.org/10.1016/j.peptides.2013.10.018

Abstract : Ghrelin is a multifunctional peptide of widespread expression. Since it has been shown to influence energy homeostatis, its potential role in thyroid dysfunction may have clinical significance. In this study, plasma ghrelin changes have been analyzed in the same patients in three different thyroid states for the first time. The study group consisted of 16 patients who had been diagnosed with hyperthyroidism, were treated with radioiodine, developed hypothyroidism after treatment, and finally became euthyroid on l-thyroxine substitution. In the initial state of hyperthyroidism plasma ghrelin levels correlated negatively with fT3 and fT4. In hypothyroidism ghrelin concentration increased significantly (p<0.05). Although the mean value of plasma ghrelin tended to decrease in the euthyroid state, the individual difference between hypothyroidism and euthyroidism was not significant. Plasma ghrelin in euthyroidism was still significantly higher than in hyperthyroidism (p<0.05), and correlated positively with ghrelin levels in hyperthyroidism and hypothyroidism. In our opinion, plasma ghrelin fluctuations may reflect metabolic changes in patients with thyroid dysfunction. Moreover, it cannot be excluded that in thyroid disorders ghrelin acts as a compensatory factor, helping to balance metabolic disturbances.