• • DRAMP ID

  • DRAMP03595

• • Peptide Name

  • Human defensin-5 (HD-5; Defensin, alpha 5; Human, mammals, animals)

• • Source

  • Homo sapiens (Human)

• • Family

  • Belongs to the alpha-defensin family

• • Gene

  • DEFA5

• • Sequence

  • ATCYCRTGRCATRESLSGVCEISGRLYRLCCR

• • Sequence Length

  • 32

• • UniProt Entry

  • Q01523,A0JDY6,Q3KNV2

• • Protein Existence

  • Protein level

• • Biological Activity

  • Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antiviral(SARS-CoV-2)

• • Target Organism

  • • [Ref.34206990]Virus:SARS-CoV-2:inhibition of infection in HEK293T-hACE2 cells(60% inhibition at 12.5 μg/mL (3.45 μM));SARS-CoV-2 variant P.1:inhibition of infection in HeLa-hACE2 cells(72% inbibition at 50 μg/mL);SARS-CoV-2 variant B.1.1.7:inhibition of infection in HeLa-hACE2 cells(32% inbibition at 50 μg/mL).
    • Gram-negative bacteria: Escherichia coli ATCC 8739 (vLD50=2.5±0.3 µg/ml), E. coli ATCC 25922 (vLD50=2.1±0.9 µg/ml), Enterobacter aerogenes ATCC 13048 (vLD50=5.5±0.5 µg/ml);
    • Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (vLD50=6.3±0.5 µg/ml), S. aureus ATCC 29213 (vLD50=3.2±0.3 µg/ml), Bacillus cereus ATCC 10876 (vLD50<0.31 µg/ml).(Ref.2)
    • NOTE: vLD50, virtual lethal doses (vLDs), equivalent to conventional 50% lethal doses (LD50s).

• • Hemolytic Activity

  • • [Ref.26206286] It has 0% hemolysis at 100μM against human red blood cells.

• • Cytotoxicity

  • • [Ref.34206990]No cytotoxicity on HEK293T cells up to 50 μg/mL.

• • Binding Target

  • Not found

• • Linear/Cyclic

  • Cyclic

• • N-terminal Modification

  • Free

• • C-terminal Modification

  • Free

• • Nonterminal Modifications and Unusual Amino Acids

  • Disulfide bonds between Cys3 and Cys31,Cys5 and Cys20,Cys10 and Cys30.

• • Stereochemistry

  • L

• • Structure

  • Beta strand

• • Structure Description

  • The L- and D-forms of HD-5 are equally active than E.coli but not S. aureus (Wei G et al 2009 JBC 284: 29180-92).

• • Helical Wheel Diagram

  • 

• • PDB ID

  • 1ZMP resolved by X-ray.
• 1ZMP-> 

• Predicted Structure

• There is no predicted structure for DRAMP03595.

DRAMP03595

• • Function

  • Antimicrobial activity against Gram-negative and Gram-positive bacteria. Defensins are thought to kill microbes by permeabilizing their plasma membrane. All DEFA5 peptides exert antimicrobial activities, but their potency is affected by peptide processing.

• • Tissue specificity

  • Paneth cells of the small intestine (at protein level).

• • PTM

  • Contains three disulfide bonds.

• ·Literature 1

• • Title

  • Human Defensins Inhibit SARS-CoV-2 Infection by Blocking Viral Entry.

• • Pubmed ID

  • 34206990

• • Reference

  • Viruses. 2021 Jun 26;13(7):1246.

• • Author

  • Xu C, Wang A, Marin M, Honnen W, Ramasamy S, Porter E, Subbian S, Pinter A, Melikyan GB, Lu W, Chang TL.

• ·Literature 2

• • Title

  • Paneth cell trypsin is the processing enzyme for human defensin-5.

• • Pubmed ID

  • 12021776

• • Reference

  • Nat Immunol. 2002 Jun;3(6):583-590.

• • Author

  • Ghosh D, Porter E, Shen B, Lee SK, Wilk D, Drazba J, Yadav SP, Crabb JW, Ganz T, Bevins CL.

• ·Literature 3

• • Title

  • Antibacterial activity and specificity of the six human {alpha}-defensins.

• • Pubmed ID

  • 15616305

• • Reference

  • Antimicrob Agents Chemother. 2005 Jan;49(1):269-275.

• • Author

  • Ericksen B, Wu Z, Lu W, Lehrer RI.

• ·Literature 4

• • Title

  • Antimicrobial activity of human -defensin 5 and its linear analogs: N-terminal fatty acylation results in enhanced antimicrobial activity of the linear analogs

• • Pubmed ID

  • 26206286

• • Reference

  • Peptides. 2015 Sep;71:128-40. doi: 10.1016/j.peptides.2015.07.009. Epub 2015 Jul 20.

• • Author

  • Basil Mathew Ramakrishnan Nagaraj