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MYP_092369
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Basic Information
PEM6
Antimicrobial
Antiviral
Antiviral ▸ Anti-HIV ▸ Anti-HIV-1
Antiviral ▸ Antiviral mechanism ▸ Viral entry inhibition
Antiviral ▸ Antiviral mechanism ▸ Viral entry inhibition ▸ Entry inhibitor
Antiviral ▸ Antiviral mechanism ▸ Viral fusion inhibition
Standard
6 amino acids
C35H54N6O9S
Standard
Sequence
PEVFLM
Physicochemical Analysis
734.90 Da
4.05
-1.04
-1.10
-0.1731
1.27
0.17
0.56
37.30
113.33
0.1667
0.00
0.00
The radar chart summarizes major physicochemical dimensions for quick comparison, while exact numerical values remain listed on the left.
Residue Composition
Amino Acid Composition
Chemical Descriptors
232.13
0.81
8.0
9.0
22.0
51.0
2.0
5.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0086047 VERIFIED: YES
Provenance & Taxonomy
Homo sapiens [Animal]
VIRIP
9606
Structure & Mods
cyclic peptide [Cyclic]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antiviral Entry inhibitor
>100 μM
IC50
PaperShort cyclic peptides derived from the C-terminal sequence of α1-antitrypsin exhibit significant anti-HIV-1 activity. PMID22406118 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/22406118/
RECORD: Rec_0091631 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
32630
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
None
None
Bio-Activity Profile
Fusion inhibition Anti-HIV-1 Antiviral Antimicrobial
HIV-1 IIIB; H9/HIV-1 IIIB cells; MT-2 cells
200 μM
Cell-cell fusion inhibition
PaperPubMed PMID: 22406118 PMID22406118 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/22406118/
RECORD: Rec_0105349 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
Protein-derived synthetic peptide
32630
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
None
None
Bio-Activity Profile
Fusion inhibition Anti-HIV-1 Antiviral
HIV-1 IIIB; H9/HIV-1 IIIB cells; MT-2 cells
200 μM
Cell-cell fusion inhibition
Mammalian: >20 h; Yeast: >20 h; E. coli: ?
PaperShort cyclic peptides derived from the C-terminal sequence of α1-antitrypsin exhibit significant anti-HIV-1 activity. | Jia Q, Jiang X, Yu F, Qiu J, Kang X, Cai L, Li L, Shi W, Liu S, Jiang S, Liu K. | Bioorg Med Chem Lett. 2012 Apr 1;22(7):2393-5. | DOI:10.1016/j.bmcl.2012.02.037 | PMID:22406118 PMID22406118 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/22406118/
RECORD: Rec_0163213 VERIFIED: NO
Provenance & Taxonomy
not reported [other]
Structure & Mods
linear peptide; DSSP H 0.0%, E 0.0%, T 16.7%, C 83.3% [Linear]
canonical L-amino-acid peptide [L]
None
None
Bio-Activity Profile
Antiviral Antimicrobial
PaperHIPdb: a database of experimentally validated HIV inhibiting peptides PMID23359817 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/23359817/
RECORD: Rec_0163594 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
32630
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
None
None
Bio-Activity Profile
Antiviral Antimicrobial
HIV-1 IIIB
100 μM
IC50
PaperPubMed PMID: 22406118 PMID22406118 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/22406118/
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