Antimicrobial Peptide AP00176






human neutrophil peptide-1 (HNP-1, HNP1, alpha Defensin, UCSS1a; lectin; primates, mammals, animals; XXX; ZZHh, BBS; BBL; BBW; 3S=S)



neutrophils; natural killer cells, monocytes; saliva; Homo sapiens








Net charge:



Hydrophobic residue%:



Boman Index:

1.07 kcal/mol


3D Structure:






SwissProt ID:

PDB ID: 3GNY   Go to PDB



anti-Gram+ & Gram-, antiviral, antifungal, antiparasitic, anti-HIV, Chemotactic, Anti-MRSA, Enzyme inhibitor, wound healing, Cancer cells


Additional info:

Activity: First alpha-defensin discovered. Active against L. monocytogenes (MIC 39.7 ug/ml), S.epidermis, S. aureus (MIC 2.2-5.2), MRSA (MIC 21.2), B. subtilis, Gram-negative E. coli, S. typhimurium, and S. maltophilia (MIC 1.8-11.9 ug/ml). HNP-1 is also active against Leishmania major promastigotes and amastigotesDabirian S et al., 2013. It can also promote wound healing. Enzyme inhibitor: it inhibits protein kinase C (Charp et al., 1988). HNP1 can also neutralize anthrax lethal toxin and other toxins (Kim C et al., 2005; Kim C et al., 2006).

Structure: The 3 disulfide bonds are between residues 2-30, 4-19, and 9-29. 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. You can rotate, zoom, and view the tetrameric crystal structure here in the PDB. There are multiple structures for HNP1 mutants or derivatives in the PDB.

MOA1: the L- and D-forms of HNP-1 (crystal structures are true mirror images) are equally active against E. coli, indicating membrane targeting. However, they displayed different activity against S. aureus. Subsequently, it was found that HNP-1 binds to cell wall precursor lipid II (dee Leeuw et al. 2010 FEBS Lett 584: 1543). MOA2: Although it is a lectin and binds to gp120 and CD4, HNP-1 was found to show inhibitory effects after HIV-1 entry (Wang et al. 2004 J Immunol 173: 515). MOA3: it inhibits non-enveloped BK virus infection by aggregating virions and blocking binding to host cells (JBC 2008; 283: 31125-31132). These examples indicate that the mechanisms of action of AMPs could depend on the type of organisms.

PTM: Arginine can be ADP-ribosylated and HNP1 became less antimicrobial and cytotoxic, thereby regulating peptide properties in vivo (Paone et al., 2002). Anti-toxin: HNP-1-3 protected mice against the fatal consequences of B. anthracis produces lethal toxin (LeTx) (Kim et al. 2005). APD Update: 12/2009; 7/2010; 12/2011; 6/2012; 10/2013; 10/2015; 9/2017; 11/2018. GW.



Primary structures of three human neutrophil defensins



Selsted ME, Harwig SS, Ganz T, Schilling JW, Lehrer RI1985



J Clin Invest. 1985 Oct;76(4):1436-9. Pub-Med.


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