Peptide name : Tr2

Source/Organism : Protein extraction from Spirulina platensis

Linear/Cyclic : Not Available

Chirality : Not Avail

Peptide length: Not available

C-terminal modification: Not Available

N-terminal modification : Not Available

Non-natural peptide information: Not Available

Assay type : MTT assay

Assay time : 48-h

Activity : IC50 < 31.25 μg/mL

Cell line : MCF-7

Cancer type : Breast Cancer

Other activity : Anticancer

Amino Acid Composition Bar Chart : Not available

Molecular mass : Not available

Aliphatic index : Not available

Instability index : Not available

Hydrophobicity (GRAVY) : Not available

Isoelectric point : Not available

Charge (pH 7) : Not available

Aromaticity : Not available

Molar extinction coefficient (cysteine, cystine): Not available

Hydrophobic/hydrophilic ratio : Not available

hydrophobic moment : Not available

Missing amino acid : Not available

Most occurring amino acid : Not available

Most occurring amino acid frequency : Not available

Least occurring amino acid : Not available

Least occurring amino acid frequency : Not available

3D-structure: Not available

Secondary structure fraction (Helix, Turn, Sheet): Not available

SMILES Notation: Not available

Molecular descriptors: Not available

ADMET properties: Not available

1 : Wang Z and Zhang X. Isolation and identification of anti-proliferative peptides from Spirulina platensis using three-step hydrolysis. J Sci Food Agric. 2017; 97:918-922. doi: 10.1002/jsfa.7815

Paper title : Isolation and identification of anti-proliferative peptides from Spirulina platensis using three-step hydrolysis.

Doi : https://doi.org/10.1002/jsfa.7815

Abstract : BACKGROUND: Spirulina platensis is an excellent source of proteins (>60%) that can be hydrolyzed into bioactive peptides. RESULTS: In this study, whole proteins of Spirulina platensis were extracted and hydrolyzed using three gastrointestinal endopeptidases (pepsin, trypsin and chymotrypsin). Subsequently, gel filtration chromatography was employed to separate hydrolysates, and four fractions (Tr1-Tr4) were obtained. Among them, Tr2 showed the strongest anti-proliferation activities on three cancer cells (MCF-7, HepG-2 and SGC-7901), with IC₅₀ values of &lt;31.25, 36.42 and 48.25 µg mL-1 , respectively. Furthermore, a new peptide, HVLSRAPR, was identified from fraction Tr1. This peptide exhibited strong inhibition on HT-29 cancer cells with an IC₅₀ value of 99.88 µg mL-1 . CONCLUSION: Taken together, these peptides possessed anti-proliferation activities on cancer cells and low cytotoxicity on normal cells, suggesting that they might serve as a natural anticancer agent for nutraceutical and pharmaceutical industries. © 2016 Society of Chemical Industry.