6k51

Structural highlights

Function

DEFPL_PSENR Antimicrobial peptide that potently acts against several species of Gram-positive bacteria (PubMed:16222292, PubMed:19472324). It selectively inhibits peptidoglycan biosynthesis through complex formation with the cell wall precursor lipid II (1:1 molar ratio) thus inhibiting cell wall synthesis (PubMed:20508130). It does not disrupt cell membranes (PubMed:20508130). Is especially active against numerous clinical isolates of S.pneumoniae, including all 90 different serotypes and isolates resistant to clinically used antibiotics (PubMed:16222292). In vitro, shows considerable selectivity for bacteria over mammalian cells (PubMed:16222292). The peptide synthesized in D-amino acids does not show antibacterial activity (PubMed:19472324). In vitro, acts on voltage-gated potassium channels by moderately inhibiting mammalian Kv1.3/KCNA3 (IC(50)=2.8 uM), and moderately inhibiting others potassium channels (PubMed:25568977).^{[1] [2]}

References

1. ↑ Mygind PH, Fischer RL, Schnorr KM, Hansen MT, Sonksen CP, Ludvigsen S, Raventos D, Buskov S, Christensen B, De Maria L, Taboureau O, Yaver D, Elvig-Jorgensen SG, Sorensen MV, Christensen BE, Kjaerulff S, Frimodt-Moller N, Lehrer RI, Zasloff M, Kristensen HH. Plectasin is a peptide antibiotic with therapeutic potential from a saprophytic fungus. Nature. 2005 Oct 13;437(7061):975-80. PMID:16222292 doi:nature04051
2. ↑ Xiang F, Xie Z, Feng J, Yang W, Cao Z, Li W, Chen Z, Wu Y. Plectasin, first animal toxin-like fungal defensin blocking potassium channels through recognizing channel pore region. Toxins (Basel). 2015 Jan 5;7(1):34-42. doi: 10.3390/toxins7010034. PMID:25568977 doi:http://dx.doi.org/10.3390/toxins7010034