Peptide name : Temporin-HLa

Source/Organism : Hylarana latouchii

Linear/Cyclic : Linear

Chirality : L

Peptide length: 17

C-terminal modification: Linear

N-terminal modification : Amidation

Non-natural peptide information:

Assay type : MTT assay

Assay time : 24-h

Activity : IC50 = 4.96 ± 0.94 μM

Cell line : NCI-H23

Cancer type : Lung Cancer

Other activity : Antimicrobial

Amino acid composition bar chart :

Molecular mass : 1876.3264 Dalton

Aliphatic index : 1.664

Instability index : 56.0706

Hydrophobicity (GRAVY) : 1.7529

Isoelectric point : 8.7501

Charge (pH 7) : 0.7591

Aromaticity : 17.64

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

Hydrophobic/hydrophilic ratio : 4.6667

hydrophobic moment : 0.5575

Missing amino acid : C,D,E,H,M,N,Q,R,T,V,W,Y

Most occurring amino acid : L

Most occurring amino acid frequency : 4

Least occurring amino acid : G

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (35., 29., 58.)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](CCCCN)NC(=O)[C@@H]1CCCN1C(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)CNC(=O)[C@H](Cc1ccccc1)NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@@H]1CCCN1C(=O)[C@H](Cc1ccccc1)NC(=O)[C@@H](N)Cc1ccccc1)[C@@H](C)CC)[C@@H](C)CC)C(=O)N[C@@H](CC(C)C)C(=O)O

1 : Lin Y, et al. Evaluation of antimicrobial and anticancer activities of three peptides identified from the skin secretion of Hylarana latouchii. Acta Biochim Biophys Sin (Shanghai). 2021; 53:1469-1483. doi: 10.1093/abbs/gmab126

Paper title : Evaluation of antimicrobial and anticancer activities of three peptides identified from the skin secretion of Hylarana latouchii.

Doi : https://doi.org/10.1093/abbs/gmab126

Abstract : The skins of frogs of the family Ranidae are particularly rich sources of biologically active peptides, among which antimicrobial peptides (AMPs) constitute the major portion. Some of these have attracted the interest of researchers because they possess both antimicrobial and anticancer activities. In this study, with 'shotgun' cloning and MS/MS fragmentation, three AMPs, homologues of family brevinin-1 (brevinin-1HL), and temporin (temporin-HLa and temporin-HLb), were discovered from the skin secretion of the broad-folded frog, Hylarana latouchii. They exhibited various degrees of antimicrobial and antibiofilm activities against test microorganisms and hemolysis on horse erythrocytes. It was found that they could induce bacteria death through disrupting cell membranes and binding to bacterial DNA. In addition, they also showed different potencies towards human cancer cell lines. The secondary structure and physicochemical properties of each peptide were investigated to preliminarily reveal their structure-activity relationships. Circular dichroism spectrometry showed that they all adopted a canonical α-helical conformation in membrane-mimetic solvents. Notably, the prepropeptide of brevinin-1HL from H. latouchii was highly identical to that of brevinin-1GHd from Hylarana guentheri, indicating a close relationship between these two species. Accordingly, this study provides candidates for the design of novel anti-infective and antineoplastic agents to fight multidrug-resistant bacteria and malignant tumors and also offers additional clues for the taxonomy of ranid frogs.