Peptide name : Varv peptide H (Varv H; Plant defensin)

Source/Organism : Field pansy

Linear/Cyclic : Cyclic

Chirality : L

Peptide length: 30

C-terminal modification: Cyclic

N-terminal modification : Not found

Non-natural peptide information: None

Assay type : Nonclonogenic fluorometric microculture cytotoxicity assay

Assay time : Not found

Activity : IC50 : >10 µg/mL

Cell line : BEL-7402

Cancer type : Leukemia

Other activity : Not found

Amino acid composition bar chart :

Molecular mass : 3079.4672 Dalton

Aliphatic index : 0.323

Instability index : 41.2567

Hydrophobicity (GRAVY) : -0.02

Isoelectric point : 4.5312

Charge (pH 7) : -1.2937

Aromaticity : 0.066

Molar extinction coefficient (cysteine, cystine): (5500, 5875)

Hydrophobic/hydrophilic ratio : 1.72727272

hydrophobic moment : 0.0209

Missing amino acid : H,Q,M,I,K,D,Y,A

Most occurring amino acid : C

Most occurring amino acid frequency : 6

Least occurring amino acid : L

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.1, 0.4, 0.3)

SMILES Notation: CC(C)C[C@H](NC(=O)CN)C(=O)N1CCC[C@H]1C(=O)N[C@H](C(=O)N[C@@H](CS)C(=O)NCC(=O)N[C@@H](CCC(=O)O)C(=O)N[C@H](C(=O)N[C@@H](CS)C(=O)N[C@@H](Cc1ccccc1)C(=O)NCC(=O)NCC(=O)N[C@H](C(=O)N[C@@H](CS)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@H](C(=O)N1CCC[C@H]1C(=O)NCC(=O)N[C@@H](CS)C(=O)N[C@@H](CO)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@H](C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N1CCC[C@H]1C(=O)N[C@H](C(=O)N[C@@H](CS)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CC(N)=O)C(=O)O)C(C)C)[C@@H](C)O)[C@@H](C)O)[C@@H](C)O)[C@@H](C)O)C(C)C

1 : Göransson U, et al. Seven novel macrocyclic polypeptides from Viola arvensis. J Nat Prod. 1999; 62:283-6. doi: 10.1021/np9803878

Paper title : Seven novel macrocyclic polypeptides from Viola arvensis.

Doi : https://doi.org/10.1021/np9803878

Abstract : Seven novel macrocyclic polypeptides, designated as varv peptides B-H, have been isolated from the aerial parts of Viola arvensis. Their primary structures have been elucidated by automated Edman degradation and mass spectrometry. They all consist of 29 or 30 amino acid residues, covalently cyclized via the amide backbone and by three internal disulfide bridges. Their amino acid sequences are as follows: varv peptide B, cyclo-(TCFGGTCNTPGCSCDPWPMCSRNGLPVCGE); varv peptide C, cyclo-(TCVGGTCNTPGCSCSWPVCTRNGVPICGE); varv peptide D, cyclo-(TCVGGSCNTPGCSCSWPVCTRNGLPICGE); varv peptide E, cyclo-(TCVGGTCNTPGCSCSWPVCTRNGLPICGE); varv peptide F, cyclo-(TCTLGTCYTAGCSCSWPVCTRNGVPICGE); varv peptide G, cyclo-(TCFGGTCNTPGCSCDPWPVCSRNGVPVCGE); and varv peptide H, cyclo-(TCFGGTCNTPGCSCETWPVCSRNGLPVCGE). The varv peptides B-H exhibited high degrees of homology with the hitherto known macrocyclic peptides varv peptide A, kalata B1, violapeptide I, circulins A and B, and cyclopsychotride A.