Peptide name : LL-37(17-29) (C-terminal fragment of LL-37, LL; Human, mammals, animals)

Source/Organism : Human

Linear/Cyclic : Not found

Chirality : Not found

Peptide length: 13

C-terminal modification: Not found

N-terminal modification : Not found

Non-natural peptide information: None

Assay type : Not specified

Assay time : Not found

Activity : Not found

Cell line : Not found

Cancer type : Not found

Other activity : Anti-microbial activity; Hemolytic activity

Amino acid composition bar chart :

Molecular mass : 1719.085 Dalton

Aliphatic index : 1.123

Instability index : 18.7

Hydrophobicity (GRAVY) : -0.438

Isoelectric point : 11.723

Charge (pH 7) : 3.7592

Aromaticity : 0.153

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

Hydrophobic/hydrophilic ratio : 0.85714285

hydrophobic moment : 2.4202

Missing amino acid : C,W,H,T,P,M,E,S,Y,N,A,G

Most occurring amino acid : R

Most occurring amino acid frequency : 3

Least occurring amino acid : V

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.2, 0.0, 0.4)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](N)Cc1ccccc1)[C@@H](C)CC)C(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(=N)N)C(=O)O

1 : Son M, et al. Disruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides. ChemMedChem. 2013; 8:1638-42. doi: 10.1002/cmdc.201300264

Paper title : Disruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides.

Doi : https://doi.org/10.1002/cmdc.201300264

Abstract : To design antimicrobial peptides with decrease pore-forming activity in eukaryotic (host) membranes, an amphipathic α-helical model peptide composed of Leu and Lys was modified to probe the balance in antimicrobial and hemolytic activities. Among analogues with broken hydrophobic interactions, L8N derivative exhibited an 8000-fold decrease in hemolytic activity and an eightfold improvement in antimicrobial activity, affording a 64 000-fold increase in therapeutic index against E. coli.