DRAVP ID  DRAVPe02128

Peptide Name   Stellettapeptin A 

Sequence  XAXYXQLGXATXQXKXQXNH

Sequence Length  12

UniProt ID  None  

Taxon ID  None 

Source  Isolated from Stelletta sponge

Validation   Experimentally Validated

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

Target Organism  HIV-1

Assay  HIV integrase inhibition assay

Activity 

• [Ref:26139946]HIV-1:EC50=23nM

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

Cytotoxicity 

• [Ref:26139946]CC50: 367 nM

Binding Target  Viral entry (Viral membrane)

Mechanism  The cyclic structure and amphipathic nature of these peptides likely enable interaction with the lipid bilayer of viral or host cell membranes.This interaction may disrupt the membrane integrity, inhibiting viral entry or replication.The peptides may interact with HIV-1 envelope proteins, preventing the virus from attaching or fusing with host cells.Some depsipeptides are known to inhibit the reverse transcriptase enzyme of HIV-1, disrupting the viral replication process.By binding to host or viral targets, the peptides may alter immune responses to enhance antiviral effects

PDB ID  None

Predicted Structure Download  No predicted structure available

Linear/Cyclic  Cyclic

N-terminal Modification  The N-terminal residue in both peptides is Hdna (3-hydroxy-6,8-dimethylnon-4-enoic acid), a unique polyketide moiety. This polyketide is linked to the peptide chain through the 3-OHAsn residue in Stel

C-terminal Modification  C-terminal is esterified to a threonine hydroxyl group, forming a cyclic structure. This ester bond is a defining feature of these cyclic depsipeptides.

Other Modification  Contains 3-OHGln and 3-OHAsn residues, rarely found in peptides.Macrocycle closure via esterification.X at position 1: N-methylalanine (NMeAla) → A (Alanine with an additional methyl group on the nitrogen),X at position 2: β-O-methyltyrosine (β-OMeTyr) → Y (Tyrosine with a methyl group on the hydroxyl group),X at position 3: N-methylglutamine (NMeGln) → Q (Glutamine with an additional methyl group on the nitrogen),X at position 4: Leucine (Unmodified),X at position 5: Glycine (Unmodified),X at p

Stereochemistry  L

Literature 1

Title   Stellettapeptins A and B, HIV-inhibitory cyclic depsipeptides from the marine sponge Stelletta sp

Pubmed ID   26139946

Reference   2015 Jul 8;56(28):4215-4219.

Author   Shin HJ, Rashid MA, Cartner LK, Bokesch HR, Wilson JA, McMahon JB, Gustafson KR. 

DOI   10.1016/j.tetlet.2015.05.058