Peptide name : Baceridin

Source/Organism : Synthetic construct

Linear/Cyclic : Cyclic

Chirality : Mix

Peptide length: Not available

C-terminal modification: Cyclic

N-terminal modification : Not found

Non-natural peptide information: None

Assay type : MTT assay

Assay time : 72h

Activity : Not found

Cell line : RKO

Cancer type : Not specified

Other activity : Anti-microbial activity

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

3D-structure: Not available

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

SMILES Notation: Not available

Molecular descriptors: Not available

ADMET properties: Not available

1 : Niggemann J, et al. Baceridin, a cyclic hexapeptide from an epiphytic bacillus strain, inhibits the proteasome. Chembiochem. 2014; 15:1021-9. doi: 10.1002/cbic.201300778

Paper title : Baceridin, a cyclic hexapeptide from an epiphytic bacillus strain, inhibits the proteasome.

Doi : https://doi.org/10.1002/cbic.201300778

Abstract : A new cyclic hexapeptide, baceridin (1), was isolated from the culture medium of a plant-associated Bacillus strain. The structure of 1 was elucidated by HR-HPLC-MS and 1D and 2D NMR experiments and confirmed by ESI MS/MS sequence analysis of the corresponding linear hexapeptide 2. The absolute configurations of the amino acid residues were determined after derivatization by GC-MS and Marfey's method. The cyclopeptide 1 consists partially of nonribosomal-derived D- and allo-D-configured amino acids. The order of the D- and L-leucine residues within the sequence cyclo(-L-Trp-D-Ala-D-allo-Ile-L-Val-D-Leu-L-Leu-) was assigned by total synthesis of the two possible stereoisomers. Baceridin (1) was tested for antimicrobial and cytotoxic activity and displayed moderate cytotoxicity (1-2 μg mL(-1)) as well as weak activity against Staphylococcus aureus. However, it was identified to be a proteasome inhibitor that inhibits cell cycle progression and induces apoptosis in tumor cells by a p53-independent pathway.