Peptide name : L11

Source/Organism : Lactoferrin

Linear/Cyclic : Cyclic

Chirality : L

Peptide length: 18

C-terminal modification: Cyclic

N-terminal modification : Free

Non-natural peptide information: None

Assay type : MTT/MTS assay

Assay time : 4h

Activity : IC50 : 116 µM

Cell line : Meth A

Cancer type : Skin cancer

Other activity : Not found

Amino acid composition bar chart :

Molecular mass : 2068.4966 Dalton

Aliphatic index : 0.55

Instability index : 29.4667

Hydrophobicity (GRAVY) : -0.694

Isoelectric point : 12

Charge (pH 7) : 5.9555

Aromaticity : 0.111

Molar extinction coefficient (cysteine, cystine): (11000, 11000)

Hydrophobic/hydrophilic ratio : 2

hydrophobic moment : -1.690

Missing amino acid : C,H,Q,T,I,E,F,S,D,Y,N,V

Most occurring amino acid : A

Most occurring amino acid frequency : 6

Least occurring amino acid : P

Least occurring amino acid frequency : 1

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

SMILES Notation: CSCC[C@H](NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](Cc1c[nH]c2ccccc12)NC(=O)[C@H](C)NC(=O)[C@H](Cc1c[nH]c2ccccc12)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)[C@@H]1CCCN1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)NCC(=O)N[C@@H](C)C(=O)O

1 : Yang N, et al. Enhanced antitumor activity and selectivity of lactoferrin-derived peptides. J Pept Res. 2002; 60:187-97. doi: 10.1034/j.1399-3011.2002.21008.x

Paper title : Enhanced antitumor activity and selectivity of lactoferrin-derived peptides.

Doi : https://doi.org/10.1034/j.1399-3011.2002.21008.x

Abstract : A number of peptide analogs derived from the N-terminal alpha-helical region of bovine lactoferrin (LFB 14-31), were designed in order to investigate how deviating numbers and positions of positively charged residues and numbers of aromatic residues affected their activity against prokaryotic, normal and transformed eukaryotic cells. Most of the LFB derivatives were highly active against both Escherichia coli and Staphylococcus aureus. The peptides were more active against the tumor cell lines MethA, HT-29 and MT-1 than normal eukaryotic cells. The peptides that were most active against the tumor cell lines had all cationic residues concentrated in one sector of the helical structure. These peptides were less selective against the tumor cell lines than against normal fibroblasts. Quantitative structure-activity relationship studies showed that certain structural parameters affected toxicity against the tumor cell lines more than against fibroblasts. Peptides encompassing these parameters were slightly less active against tumor cells, but gained significant selectivity.