Structural highlights
Function
OCEF1_LEPLB Antibacterial peptide that inhibits reference strains of both Gram-negative bacteria (E.coli, P.aeruginosa, E.cloacae, K.pneumoniae, and A.actinomycetemcomitans) and Gram-positive bacteria (S.aureus) with relatively low potencies (MIC=25-400 uM) (By similarity) (PubMed:28115922). Shows antifungal activity against C.lusitaniae (MIC=50.25 uM), but no activity against C.albicans (PubMed:28115922). In the presence of an alkaloid (bufotenine), inhibits cellular infection by the rabies virus (PubMed:26635873). The peptide shows very low hemolytic activity against rabbit erythrocytes (By similarity) (PubMed:28115922). The low amphipathicity of alpha-helices demonstrated by wheel projection as well as the low cationicity may explain the low antibacterial and hemolytic potencies (By similarity).[UniProtKB:P0DQJ8][1] [2]
References
- ↑ Cunha Neto Rdos S, Vigerelli H, Jared C, Antoniazzi MM, Chaves LB, da Silva Ade C, Melo RL, Sciani JM, Pimenta DC. Synergic effects between ocellatin-F1 and bufotenine on the inhibition of BHK-21 cellular infection by the rabies virus. J Venom Anim Toxins Incl Trop Dis. 2015 Dec 2;21:50. PMID:26635873 doi:10.1186/s40409-015-0048-1
- ↑ Gusmão KAG, Dos Santos DM, Santos VM, Cortés ME, Reis PVM, Santos VL, Piló-Veloso D, Verly RM, de Lima ME, Resende JM. Ocellatin peptides from the skin secretion of the South American frog Leptodactylus labyrinthicus (Leptodactylidae): characterization, antimicrobial activities and membrane interactions. J Venom Anim Toxins Incl Trop Dis. 2017 Jan 19;23:4. PMID:28115922 doi:10.1186/s40409-017-0094-y
