General Information


DRAVP ID  DRAVPe02130

Peptide Name   Mollamide E

Sequence  XFPSLTCLSTXC

Sequence Length  10

UniProt ID  None  

Taxon ID  None 

Source  Tunicate Didemnum molle PNG07-2-050

Validation   Experimentally Validated



Origin Information


Gene Name/ID  Not Available

GenBank  Not Available

Amino Acid position  Not Available

Domain Accession ID  Not Available

Nucleotide sequence ID  Not Available

Molecular Type  Not Available

Chromosomal Position  Not Available



Activity Information


Target Organism  HIV-1

Assay  HIV integrase inhibition assay and cytoprotective cell-based assay

Activity 

  • [Ref:22845329]HIV-1:No inhibition at78μM;NoHIV integrase inhibition at 100μg/mL

Hemolytic Activity  No hemolysis information or data found in the reference(s) presented in this entry

Cytotoxicity  No cytotoxicity information found in the reference(s) presented

Binding Target  Viral integrase

Mechanism  Mollamide E does not exhibit significant HIV inhibition activity in cytoprotective or integrase assays. Its mechanism of action remains uncharacterized but may involve steric or structural features that prevent integrase binding, unlike its analog Mollamide F



Structure Information


PDB ID  None

Predicted Structure Download  No predicted structure available

Linear/Cyclic  Cyclic

N-terminal Modification  Phenylalanine (Phe)

C-terminal Modification  Thiazoline (Cys-derived residue)

Other Modification  The cysteine residue forms a thiazoline ring, contributing to the rigidity and cyclic nature of the peptide.Attached to the threonine residue, this modification is a unique structural feature.Contains d-Phe and d-thiazoline, resulting from thermodynamic relaxation under constrained peptide geometry.X at position 1: D-Phenylalanine (D-Phe) → Mirror image of L-Phe, not commonly found in natural peptides, X at position 7: D-Cysteine in thiazoline ring → Modified residue, involved in heterocyclic st

Stereochemistry  L



Physicochemical Information


Formula  C35H50N6O7S

Absent amino acids  ARNDQEGHIKMWYVOU

Common amino acids  CLST

Mass  1071.27

Pl  5.51

Basic residues  0

Acidic residues  0

Hydrophobic residues  8

Net charge  0

Boman Index  0.96

Hydrophobicity  1.08

Aliphatic Index  78

Half Life 

  •     Mammalian:1.1hours
  •     Yeast:3 min
  •     E.coli:2 min

Extinction Coefficient cystines  0

Absorbance 280nm  0

Polar residues  8



Literature Information


Literature 1

Title   Thiazoline Peptides and a Tris-Phenethyl Urea from Didemnum molle with Anti-HIV Activity

Pubmed ID   22845329

Reference   J Nat Prod. 2012 Aug 24;75(8):1436-40.

Author   Lu Z, Harper MK, Pond CD, Barrows LR, Ireland CM, Van Wagoner RM.

DOI   10.1021/np300270p