Peptide name : Peptide 3a

Source/Organism : Synthetic

Linear/Cyclic : Linear

Chirality : L

Peptide length: 2

C-terminal modification: Linear

N-terminal modification : Free

Non-natural peptide information:

Assay type : MTT assay

Assay time : 48-h

Activity : IC50 = 5.7 ± 0.04 µM

Cell line : A-549

Cancer type : Lung Cancer

Other activity : Antiproliferative, Anticancer

Amino acid composition bar chart :

Molecular mass : 296.2759 Dalton

Aliphatic index : 0

Instability index : 123.4

Hydrophobicity (GRAVY) : -2.4

Isoelectric point : 4.2994

Charge (pH 7) : -1.2366

Aromaticity : 50

Molar extinction coefficient (cysteine, cystine): (0, 0)

Hydrophobic/hydrophilic ratio : 0

hydrophobic moment : -0.346

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

Most occurring amino acid : Y

Most occurring amino acid frequency : 1

Least occurring amino acid : Y

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0, 50, 50)

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

1 : Ahmaditaba MA, et al. Design, Synthesis, and Biological Evaluation of New Peptide Analogues as Selective COX-2 Inhibitors. Arch Pharm (Weinheim). 2017; 350:(unknown pages). doi: 10.1002/ardp.201700158

Paper title : Design, Synthesis, and Biological Evaluation of New Peptide Analogues as Selective COX-2 Inhibitors.

Doi : https://doi.org/10.1002/ardp.201700158

Abstract : A new class of peptide derivatives possessing SO₂ Me and N₃ pharmacophores at the para position of a phenyl ring bound to different aromatic amino acids were synthesized based on solid-phase synthesis methodology, and evaluated as selective cyclooxygenase-2 (COX-2) inhibitors. One of the analogues, i.e., compound 2a as the representative of this series, was recognized as the highest selective COX-2 inhibitor with a COX-2 selectivity index of >500. The structure-activity relationships (SARs) acquired indicated that compound 2a containing a 4-(methylsulfonyl)benzoyl group as a pharmacophore and tyrosine as a ring bearing amino acid in the second position and glutamic acid as the C-terminal amino acid can give the essential geometry to provide selective COX-2 inhibitory activity. Antiproliferative activity of the synthesized peptides (1a-7b) was also determined against four different human cancer cell lines, including MCF-7, HepG2, A549, and HeLa. According to our results, A549, HepG2, and MCF7 seemed to be more sensitive cell lines than HeLa cells encountering these compounds, which gave inhibitory action with IC₅₀ values from 4.8 to 64.4 µM. In this regard, compounds 3a and 2b displayed the best inhibitory activity against the cell lines. Moreover, a good correlation was observed between the antiproliferative potency and the COX-2 inhibitory activity of compounds 1a, 2a, 2b, and 5b. Such findings suggest that one of the mechanism of anticancer activity of these peptides may be through the COX-2 inhibitory action.