dbACP: A Comprehensive Database of Anti-Cancer Peptides

dbacp06225

General Description

Peptide name : Temporin 1OLa

Source/Organism : Florida bog frog, North America

Linear/Cyclic : Cyclic

Chirality : Not found

Sequence Information

Sequence : FLPFLKSILGKIL

Peptide length: 13

C-terminal modification: Cyclic

N-terminal modification : Free

Non-natural peptide information: None

Activity Information

Assay type : Not specified

Assay time : Not found

Activity : Not found

Cell line : Not found

Cancer type : Not found

Other activity : Anti- microbial activity

Physicochemical Properties

Amino acid composition bar chart :

Molecular mass : 1488.8969 Dalton

Aliphatic index : 1.8

Instability index : 48.9

Hydrophobicity (GRAVY) : 1.4769

Isoelectric point : 10.002

Charge (pH 7) : 1.7581

Aromaticity : 0.153

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

Hydrophobic/hydrophilic ratio : 3.33333333

hydrophobic moment : 1.4063

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

Most occurring amino acid : L

Most occurring amino acid frequency : 4

Least occurring amino acid : P

Least occurring amino acid frequency : 1

Structural Information

3D structure :

Secondary structure fraction (Helix, Turn, Sheet): (0.4, 0.2, 0.6)

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

Secondary Structure :

Method Prediction
GOR CCHHHHHHHTEEE
Chou-Fasman (CF) CCCCEEEEEECCC
Neural Network (NN) CCCHHHHHCCHHH
Joint/Consensus CCCHHHHHCCCCC

Molecular Descriptors and ADMET Properties

Molecular Descriptors: Click here to download

ADMET Properties: Click here to download

Cross Referencing databases

Pubmed Id : 17005262

Uniprot : Not available

PDB : Not available

CancerPPD : Not available

ApIAPDB : Not available

CancerPPD2 ID : Not available

Reference

1 : Conlon JM, et al. Peptidomic analysis of skin secretions from Rana heckscheri and Rana okaloosae provides insight into phylogenetic relationships among frogs of the Aquarana species group. Regul Pept. 2007; 138:87-93. doi: 10.1016/j.regpep.2006.08.007

Literature

Paper title : Peptidomic analysis of skin secretions from Rana heckscheri and Rana okaloosae provides insight into phylogenetic relationships among frogs of the Aquarana species group.

Doi : https://doi.org/10.1016/j.regpep.2006.08.007

Abstract : The members of the Aquarana (or Rana catesbeiana species group) form a monophyletic group comprising seven species: R. catesbeiana, Rana clamitans, Rana grylio, Rana virgatipes, Rana septentrionalis, Rana heckscheri and Rana okaloosae. Previous work has led to structural characterization of the antimicrobial peptides present in electrically-stimulated skin secretions from the first five species listed and this study presents the primary structures of orthologs from the river frog R. heckscheri and the Florida bog frog R. okaloosae. Peptidomic analysis of R. heckscheri and R. okaloosae skin secretions led to the identification of peptides with antimicrobial activity belonging to the ranalexin, ranatuerin-2, and temporin families. In addition, a peptide (GFLDIIKDTGKDFAVKILNNLKCKLAGGCPR) was isolated from R. okaloosae whose primary structure identified it as a member of the palustrin-2 family. Consistent with previous data based upon morphological analysis and comparisons of the nucleotide sequences of mitochondrial and ribosomal genes, cladistic analysis based upon a comparison of the amino acid sequences of antimicrobial peptides indicates a sister-group relationship between R. heckscheri and R. grylio and a close, but less well defined, phylogenetic relationship between R. okaloosae and R. clamitans.