dbACP: A Comprehensive Database of Anti-Cancer Peptides

dbacp06821

General Description

Peptide name : [C/U]cGm

Source/Organism : Synthetic Analogue of Gomesin

Linear/Cyclic : Cyclic

Chirality : L

Sequence Information

Sequence : GURRLUYKQRUVTYURGR

Peptide length: Not available

C-terminal modification: Cyclic

N-terminal modification : Cyclized

Non-natural peptide information: U = SelenoCys

Activity Information

Assay type : Resazurin dye assay

Assay time : 24-h

Activity : CC50 > 64 μM

Cell line : HeLa

Cancer type : Cervical Cancer

Other activity : Antimicrobial

Physicochemical Properties

Amino Acid Composition Bar Chart : Not available

Molecular mass : Not available

Aliphatic index : Not available

Instability index : Not available

Hydrophobicity (GRAVY) : Not available

Isoelectric point : Not available

Charge (pH 7) : Not available

Aromaticity : Not available

Molar extinction coefficient (cysteine, cystine): Not available

Hydrophobic/hydrophilic ratio : Not available

hydrophobic moment : Not available

Missing amino acid : Not available

Most occurring amino acid : Not available

Most occurring amino acid frequency : Not available

Least occurring amino acid : Not available

Least occurring amino acid frequency : Not available

Structural Information

3D-structure: Not available

Secondary structure fraction (Helix, Turn, Sheet): Not available

SMILES Notation: Not available

Secondary Structure :

Method Prediction
GOR Not available
Chou-Fasman (CF) Not available
Neural Network (NN) Not available
Joint/Consensus Not available

Molecular Descriptors and ADMET Properties

Molecular descriptors: Not available

ADMET properties: Not available

Cross Referencing Databases databases

Pubmed Id : 36982972.0, .

Uniprot : Not available

CancerPPD : Not available

ApIAPDB : Not available

Reference

1 : Liu X, et al. Unlocking the Potential of the Antimicrobial Peptide Gomesin: From Discovery and Structure-Activity Relationships to Therapeutic Applications. Int J Mol Sci. 2023; 24:(unknown pages). doi: 10.3390/ijms24065893

Literature

Paper title : Unlocking the Potential of the Antimicrobial Peptide Gomesin: From Discovery and Structure-Activity Relationships to Therapeutic Applications.

Doi : https://doi.org/10.3390/ijms24065893

Abstract : Gomesin is a cationic antimicrobial peptide which is isolated from the haemocytes of the Brazilian tarantula Acanthoscurria gomesiana and can be produced chemically by Fmoc solid-phase peptide synthesis. Gomesin exhibits a range of biological activities, as demonstrated by its toxicity against therapeutically relevant pathogens such as Gram-positive or Gram-negative bacteria, fungi, cancer cells, and parasites. In recent years, a cyclic version of gomesin has been used for drug design and development as it is more stable than native gomesin in human serum and can penetrate and enter cancer cells. It can therefore interact with intracellular targets and has the potential to be developed as a drug lead for to treat cancer, infectious diseases, and other human diseases. This review provides a perspective on the discovery, structure-activity relationships, mechanism of action, biological activity, and potential clinical applications of gomesin.