• • DRAMP ID

  • DRAMP03591

• • Peptide Name

  • Neutrophil defensin 1 (Defensin, alpha 1; HNP-1, HP-1; Human, mammals, animals)

• • Source

  • Homo sapiens (Human)

• • Family

  • Belongs to the alpha-defensin family

• • Gene

  • DEFA1, DEFA1B

• • Sequence

  • ACYCRIPACIAGERRYGTCIYQGRLWAFCC

• • Sequence Length

  • 30

• • UniProt Entry

  • P59665,P11479,Q14125,Q6EZF6

• • 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(approximately 50% inbibition at 1 μg/mL (290 nM));SARS-CoV-2 variant P.1:inhibition of infection in HeLa-hACE2 cells(67% inbibition at 50 μg/mL);SARS-CoV-2 variant B.1.1.7:inhibition of infection in HeLa-hACE2 cells(58% inbibition at 50 μg/mL).
    • [Ref.15616305] Gram-negative bacteria: Escherichia coli ATCC 8739 (vLD50=3.6±0.3 μg/ml), E. coli ATCC 25922 (vLD50=3.7±0.4 μg/ml), Enterobacter aerogenes ATCC 13048 (vLD50=10±0.5 μg/ml);
    • Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (vLD50=4.2±1.0 μg/ml), Staphylococcus aureus ATCC 29213 (vLD50=2.1±0.3 μg/ml), Bacillus cereus ATCC 10876 (vLD50=0.22±0.03 μg/ml).
    • NOTE: vLD50, virtual lethal doses (vLDs), equivalent to conventional 50% lethal doses (LD50s).
    • [Ref.15118082]Gram-positive bacteria: Bacillus subtilis (Inhibition zone=24 mm in PH5.5, Inhibition zone=20 mm in PH7.5 completely inhibit at 10 μg/well), Staphylococcus aureus (Inhibition zone=1 mm in PH5.5, Inhibition zone=7 mm incompletely inhibit and Inhibition zone=2 mm completely inhibit in PH7.5 at 10 μg/well);
    • Gram-negative bacteria: Escherichia coli (Inhibition zone=5 mm incompletely inhibit and Inhibition zone=2 mm completely inhibit in PH7.5 at 10 μg/well);
    • Fungi: Candida albicans (Inhibition zone=13 mm in PH5.5, Inhibition zone=10 mm in PH7.5 completely inhibit at 10 μg/well).

• • Hemolytic Activity

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

• • 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

  • Cyclization(Cys2 and Cys30).

• • Nonterminal Modifications and Unusual Amino Acids

  • Disulfide bonds between Cys2 and Cys30,Cys4 and Cys19,Cys9 and Cys29.

• • Stereochemistry

  • L

• • Structure

  • Beta strand

• • Structure Description

  • Compared to HNP-2, HNP-1 contains one additional residue (Ala) at the N-terminus. It contains a long stretch of a double-stranded antiparallel beta-sheet in a hairpin conformation that contains a beta-bulge, a short region of triple-stranded beta-sheet, and several tight turns.

• • Helical Wheel Diagram

  • 

• • PDB ID

  • 2KHT resolved by NMR
• 2KHT-> 

• Predicted Structure

• There is no predicted structure for DRAMP03591.

DRAMP03591

• • Function

  • Defensin 1 and defensin 2 have antibacterial, fungicide and antiviral activities. Has antimicrobial activity against Gram-negative and Gram-positive bacteria. Defensins are thought to kill microbes by permeabilizing their plasma membrane.

• • PTM

  • ADP-ribosylation drastically reduces cytotoxic and antibacterial activities, and enhances IL8 production. Phosphorylation at Tyr-85 has been found in some cancer cell lines, and interferes with ADP-rybosylation.

• ·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

  • Isolation, purification and de novo sequencing of TBD-1, the first beta-defensin from leukocytes of reptiles.

• • Pubmed ID

  • 19253295

• • Reference

  • Proteomics. 2009 Mar;9(5):1364-1373.

• • Author

  • Stegemann C, Kolobov A Jr, Leonova YF, Knappe D, Shamova O, Ovchinnikova TV, Kokryakov VN, Hoffmann R.

• ·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

  • Multidimensional signatures in antimicrobial peptides.

• • Pubmed ID

  • 15118082

• • Reference

  • Proc Natl Acad Sci U S A. 2004 May 11;101(19):7363-8.

• • Author

  • Yount NY, Yeaman MR.