Peptide name : Distinctin-Like-Peptide-PH

Source/Organism : Skin Secretion, Northern orange-legged leaf frog, South America

Linear/Cyclic : Not found

Chirality : Not found

Peptide length: 36

C-terminal modification: Not found

N-terminal modification : Free

Non-natural peptide information: None

Assay type : MTT Cell viability assay, LDH assay

Assay time : 24h

Activity : IC50 : 32.25 μg/mL

Cell line : PC3

Cancer type : Lung cancer

Other activity : Anti-microbial activity

Amino acid composition bar chart :

Molecular mass : 4196.8977 Dalton

Aliphatic index : 0.975

Instability index : 19.0722

Hydrophobicity (GRAVY) : -1.197

Isoelectric point : 10.359

Charge (pH 7) : 7.7585

Aromaticity : 0.027

Molar extinction coefficient (cysteine, cystine): (1490, 1490)

Hydrophobic/hydrophilic ratio : 0.5

hydrophobic moment : -0.375

Missing amino acid : C,W,H,Q,T,P,M,F,D

Most occurring amino acid : K

Most occurring amino acid frequency : 9

Least occurring amino acid : I

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.5, 0.2, 0.2)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](N)CC(N)=O)C(C)C)C(=O)N[C@@H](CCC(=O)O)C(=O)NCC(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(N)=O)C(=O)O)C(C)C

1 : Wu D, et al. Discovery of Distinctin-Like-Peptide-PH (DLP-PH) From the Skin Secretion of Phyllomedusa hypochondrialis, a Prototype of a Novel Family of Antimicrobial Peptide. Front Microbiol. 2018; 9:541. doi: 10.3389/fmicb.2018.00541

Paper title : Discovery of Distinctin-Like-Peptide-PH (DLP-PH) From the Skin Secretion of Phyllomedusa hypochondrialis, a Prototype of a Novel Family of Antimicrobial Peptide.

Doi : https://doi.org/10.3389/fmicb.2018.00541

Abstract : Amphibian skin secretions are an important treasure house of bioactive antimicrobial peptides (AMPs). Despite having been the focus of decades of research in this context, investigations of phyllomedusine frogs continue to identify new AMPs from their skin secretions. In this study, the prototype of a novel family of AMP distinctin-like-peptide-PH (DLP-PH) was identified from the skin secretion of the otherwise well-studied Tiger-Legged Tree Frog Phyllomedusa hypochondrialis through cloning of its precursor-encoding cDNA from a skin secretion-derived cDNA library by a 3'-rapid amplification of cDNA ends (RACE) strategy. Subsequently, the mature peptide was isolated and characterized using reverse-phase HPLC and MS/MS fragmentation sequencing. DLP-PH adopted an α-helical conformation in membrane mimetic solution and demonstrated unique structural features with two distinct domains that differed markedly in their physiochemical properties. Chemically synthesized replicates of DLP-PH showed antimicrobial activity against planktonic bacterial and yeast cells, but more potent against Escherichia coli at 32 μg/mL. However, DLP-PH showed much weaker inhibitory activity against the growth of sessile cells in biofilms. In addition, DLP-PH exhibited anti-proliferative activity against human cancer cell lines, H157, and PC3, but with no major toxicity against normal human cell, HMEC-1. These combined properties make DLP-PH deserving further study as an antimicrobial agent and further investigations of its structure-activity relationship could provide valuable new insights into drug lead candidates for antimicrobial and/or anti-cancer purposes.