| Structural highlights
Function
PROTO_POLPI Potent antimicrobial peptide that acts by disrupting bacterial membrane (PubMed:21745529, PubMed:22450985). Is active against both Gram-positive and Gram-negative bacteria (B.subtilis (MIC=15 ug/ml or 4-16 uM), S.epidermidis (MIC=8-16 uM), S.aureus (MIC=15 ug/ml or 4 uM), E.coli (MIC=8-64 uM) and P.aeruginosa (MIC=64-128 uM)) (PubMed:16129513, PubMed:22450985, PubMed:23836163, PubMed:30534613). Also shows cytotoxicity towards HEK293 cells (32 uM) (PubMed:30534613). Adopts an amphipathic alpha helical conformation, that may allow to partition into the target membrane (PubMed:21745529, PubMed:23836163). Also acts in inflammation since it is chemotactic for polymorphonucleated leukocytes (PMNL) (PubMed:16129513). Shows potent antitumor activity against prostate (PC-3) and bladder (Biu-87) cancer cell lines (PubMed:21745529). Causes a reduced hemolysis to mammalian erythrocytes (HC(50)=50 uM) and has no mast cell degranulation activity at physiological concentrations (PubMed:16129513, PubMed:30534613). In addition, when tested in vitro on the parasite Trypanosoma cruzi (responsible of the Chagas disease), is able to reduce the number of the three forms (epimastigote, trypomastigote and amastigote), probably acting through the apoptotic cell death pathway (PubMed:32360153).[1] [2] [3] [4] [5] [6]
References
- ↑ Souza BM, Mendes MA, Santos LD, Marques MR, Cesar LM, Almeida RN, Pagnocca FC, Konno K, Palma MS. Structural and functional characterization of two novel peptide toxins isolated from the venom of the social wasp Polybia paulista. Peptides. 2005 Nov;26(11):2157-64. doi: 10.1016/j.peptides.2005.04.026. Epub 2005 , Aug 29. PMID:16129513 doi:https://dx.doi.org/10.1016/j.peptides.2005.04.026
- ↑ Wang K, Yan J, Liu X, Zhang J, Chen R, Zhang B, Dang W, Zhang W, Kai M, Song J, Wang R. Novel cytotoxity exhibition mode of polybia-CP, a novel antimicrobial peptide from the venom of the social wasp Polybia paulista. Toxicology. 2011 Oct 9;288(1-3):27-33. doi: 10.1016/j.tox.2011.06.014. Epub 2011 , Jul 1. PMID:21745529 doi:https://dx.doi.org/10.1016/j.tox.2011.06.014
- ↑ Wang K, Yan J, Chen R, Dang W, Zhang B, Zhang W, Song J, Wang R. Membrane-active action mode of polybia-CP, a novel antimicrobial peptide isolated from the venom of Polybia paulista. Antimicrob Agents Chemother. 2012 Jun;56(6):3318-23. doi: 10.1128/AAC.05995-11. , Epub 2012 Mar 26. PMID:22450985 doi:https://dx.doi.org/10.1128/AAC.05995-11
- ↑ Wang K, Dang W, Yan J, Chen R, Liu X, Yan W, Zhang B, Xie J, Zhang J, Wang R. Membrane perturbation action mode and structure-activity relationships of Protonectin, a novel antimicrobial peptide from the venom of the neotropical social wasp Agelaia pallipes pallipes. Antimicrob Agents Chemother. 2013 Oct;57(10):4632-9. doi: 10.1128/AAC.02311-12., Epub 2013 Jul 8. PMID:23836163 doi:https://dx.doi.org/10.1128/AAC.02311-12
- ↑ Torres MDT, Pedron CN, Higashikuni Y, Kramer RM, Cardoso MH, Oshiro KGN, Franco OL, Silva Junior PI, Silva FD, Oliveira Junior VX, Lu TK, de la Fuente-Nunez C. Structure-function-guided exploration of the antimicrobial peptide polybia-CP identifies activity determinants and generates synthetic therapeutic candidates. Commun Biol. 2018 Dec 7;1:221. doi: 10.1038/s42003-018-0224-2. eCollection 2018. PMID:30534613 doi:https://dx.doi.org/10.1038/s42003-018-0224-2
- ↑ Freire KA, Torres MT, Lima DB, Monteiro ML, Bezerra de Menezes RRPP, Martins AMC, Oliveira VX Jr. Wasp venom peptide as a new antichagasic agent. Toxicon. 2020 Jul 15;181:71-78. doi: 10.1016/j.toxicon.2020.04.099. Epub 2020 Apr , 28. PMID:32360153 doi:https://dx.doi.org/10.1016/j.toxicon.2020.04.099
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