Peptide name : HECI

Source/Organism : Hylarana erythraea

Linear/Cyclic : Not found

Chirality : Not found

Peptide length: 17

C-terminal modification: Not found

N-terminal modification : Amidation

Non-natural peptide information: None

Assay type : MTT anti-proliferation assay

Assay time : 24h

Activity : MIC : 1µM

Cell line : PC-3

Cancer type : Prostate cancer

Other activity : Not found

Amino acid composition bar chart :

Molecular mass : 1952.3448 Dalton

Aliphatic index : 0.629

Instability index : 41.8824

Hydrophobicity (GRAVY) : 0.3765

Isoelectric point : 8.9366

Charge (pH 7) : 1.3774

Aromaticity : 0.176

Molar extinction coefficient (cysteine, cystine): (5500, 5625)

Hydrophobic/hydrophilic ratio : 2.4

hydrophobic moment : -0.578

Missing amino acid : H,Q,M,E,D,Y,N,A

Most occurring amino acid : P

Most occurring amino acid frequency : 3

Least occurring amino acid : V

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.1, 0.2, 0.4)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](CS)NC(=O)[C@@H]1CCCN1C(=O)[C@H](CCCCN)NC(=O)[C@@H]1CCCN1C(=O)[C@@H]1CCCN1C(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](CO)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@@H](NC(=O)[C@H](Cc1c[nH]c2ccccc12)NC(=O)[C@H](CS)NC(=O)CNC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@@H](N)[C@@H](C)O)C(C)C)[C@@H](C)O)C(=O)O

1 : Zhang L, et al. A Bowman-Birk type chymotrypsin inhibitor peptide from the amphibian, Hylarana erythraea. Sci Rep. 2018; 8:5851. doi: 10.1038/s41598-018-24206-4

Paper title : A Bowman-Birk type chymotrypsin inhibitor peptide from the amphibian, Hylarana erythraea.

Doi : https://doi.org/10.1038/s41598-018-24206-4

Abstract : The first amphibian skin secretion-derived Bowman-Birk type chymotrypsin inhibitor is described here from the Asian green frog, Hylarana erythraea, and was identified by use of molecular cloning and tandem mass spectrometric amino acid sequencing. It was named Hylarana erythraea chymotrypsin inhibitor (HECI) and in addition to inhibition of chymotrypsin (Ki = 3.92 ± 0.35 μM), the peptide also inhibited the 20 S proteasome (Ki = 8.55 ± 1.84  μM). Additionally, an analogue of HECI, named K9-HECI, in which Phe9 was substituted by Lys9 at the P1 position, was functional as a trypsin inhibitor. Both peptides exhibited anti-proliferation activity against the human cancer cell lines, H157, PC-3 and MCF-7, up to a concentration of 1 mM and possessed a low degree of cytotoxicity on normal cells, HMEC-1. However, HECI exhibited higher anti-proliferative potency against H157. The results indicate that HECI, inhibiting chymotryptic-like activity of proteasome, could provide new insights in treatment of lung cancer.