Peptide name : Cyclosaplin

Source/Organism : Not found

Linear/Cyclic : Cyclic

Chirality : Not found

Peptide length: 8

C-terminal modification: Cyclic

N-terminal modification : Free

Non-natural peptide information: None

Assay type : DNA fragmentation assay

Assay time : 24h

Activity : IC50 : 2.06 µg/mL

Cell line : MDA-MB-231

Cancer type : Breast cancer

Other activity : Not found

Amino acid composition bar chart :

Molecular mass : 876.9811 Dalton

Aliphatic index : 0.487

Instability index : 49.5

Hydrophobicity (GRAVY) : -0.962

Isoelectric point : 8.2495

Charge (pH 7) : 0.7513

Aromaticity : 0

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

Hydrophobic/hydrophilic ratio : 1

hydrophobic moment : -1.579

Missing amino acid : W,H,Q,P,M,I,E,K,S,F,Y,N,A,V

Most occurring amino acid : R

Most occurring amino acid frequency : 2

Least occurring amino acid : L

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.1, 0.3, 0.2)

SMILES Notation: CC(C)C[C@H](NC(=O)[C@@H](N)CCCNC(=N)N)C(=O)NCC(=O)N[C@@H](CC(=O)O)C(=O)NCC(=O)N[C@@H](CS)C(=O)N[C@H](C(=O)N[C@@H](CCCNC(=N)N)C(=O)O)[C@@H](C)O

1 : Mishra A, et al. Identification and structural characterization of a new pro-apoptotic cyclic octapeptide cyclosaplin from somatic seedlings of Santalum album L. Peptides. 2014; 54:148-58. doi: 10.1016/j.peptides.2014.01.023

Paper title : Identification and structural characterization of a new pro-apoptotic cyclic octapeptide cyclosaplin from somatic seedlings of Santalum album L.

Doi : https://doi.org/10.1016/j.peptides.2014.01.023

Abstract : Small cyclic peptides exhibiting potent biological activity have great potential for anticancer therapy. An antiproliferative cyclic octapeptide, cyclosaplin was purified from somatic seedlings of Santalum album L. (sandalwood) using gel filtration and RP-HPLC separation process. The molecular mass of purified peptide was found to be 858 Da and the sequence was determined by MALDI-ToF-PSD-MS as 'RLGDGCTR' (cyclic). The cytotoxic activity of the peptide was tested against human breast cancer (MDA-MB-231) cell line in a dose and time-dependent manner. The purified peptide exhibited significant antiproliferative activity with an IC50 2.06 μg/mL. In a mechanistic approach, apoptosis was observed in differential microscopic studies for peptide treated MDA-MB-231 cells, which was further confirmed by mitochondrial membrane potential, DNA fragmentation assay, cell cycle analysis and caspase 3 activities. The modeling and docking experiments revealed strong affinity (kcal/mol) of peptide toward EGFR and procaspase 3. The co-localization studies revealed that the peptide sensitizes MDA-MB-231 cells by possibly binding to EGFR and induces apoptosis. This unique cyclic octapeptide revealed to be a favorable candidate for development of anticancer agents.