Peptide name : αs1-casein f(90_95)

Source/Organism : Bovine milk

Linear/Cyclic : Linear

Chirality : L

Peptide length: 6

C-terminal modification: Linear

N-terminal modification : Amidation

Non-natural peptide information: None

Assay type : MTT/MTS assay

Assay time : Not found

Activity : Inhibition at 12 - 15 g/l

Cell line : AZ-97

Cancer type : Colon cancer

Other activity : Immunomodulatory activity; Antihypertensive activity; Anti-microbial acivity; Antiviral activity; Antioxidant activity

Amino acid composition bar chart :

Molecular mass : 783.9139 Dalton

Aliphatic index : 1.3

Instability index : -18.383

Hydrophobicity (GRAVY) : 0.0167

Isoelectric point : 8.5897

Charge (pH 7) : 0.7581

Aromaticity : 0.333

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

Hydrophobic/hydrophilic ratio : 1

hydrophobic moment : -1.992

Missing amino acid : W,T,P,I,M,E,K,F,D,N,C,H,Q,S,A,V

Most occurring amino acid : Y

Most occurring amino acid frequency : 2

Least occurring amino acid : R

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.3, 0.1, 0.6)

SMILES Notation: CC(C)C[C@H](NC(=O)[C@H](Cc1ccc(O)cc1)NC(=O)CNC(=O)[C@H](CC(C)C)NC(=O)[C@H](Cc1ccc(O)cc1)NC(=O)[C@@H](N)CCCNC(=N)N)C(=O)O

1 : Pepe G, et al. Potential anticarcinogenic peptides from bovine milk. J Amino Acids. 2013; 2013:939804. doi: 10.1155/2013/939804

Paper title : Potential anticarcinogenic peptides from bovine milk.

Doi : https://doi.org/10.1155/2013/939804

Abstract : BOVINE MILK POSSESSES A PROTEIN SYSTEM CONSTITUTED BY TWO MAJOR FAMILIES OF PROTEINS: caseins (insoluble) and whey proteins (soluble). Caseins ( α S1, α S2, β , and κ ) are the predominant phosphoproteins in the milk of ruminants, accounting for about 80% of total protein, while the whey proteins, representing approximately 20% of milk protein fraction, include β -lactoglobulin, α -lactalbumin, immunoglobulins, bovine serum albumin, bovine lactoferrin, and lactoperoxidase, together with other minor components. Different bioactivities have been associated with these proteins. In many cases, caseins and whey proteins act as precursors of bioactive peptides that are released, in the body, by enzymatic proteolysis during gastrointestinal digestion or during food processing. The biologically active peptides are of particular interest in food science and nutrition because they have been shown to play physiological roles, including opioid-like features, as well as immunomodulant, antihypertensive, antimicrobial, antiviral, and antioxidant activities. In recent years, research has focused its attention on the ability of these molecules to provide a prevention against the development of cancer. This paper presents an overview of antitumor activity of caseins and whey proteins and derived peptides.