Otro
Chemical and biological characterization of four new linear cationic α-helical peptides from the venoms of two solitary eumenine wasps
Registro en:
Toxicon, v. 57, n. 7-8, p. 1081-1092, 2011.
0041-0101
1879-3150
10.1016/j.toxicon.2011.04.014
2-s2.0-79956338547.pdf
2-s2.0-79956338547
Autor
Rangel, Marisa
dos Santos Cabrera, Marcia Perez
Kazuma, Kohei
Ando, Kenji
Wang, Xiaoyu
Kato, Manabu
Nihei, Ken-ichi
Hirata, Izaura Yoshico
Cross, Tyra J.
Garcia, Angélica Nunes
Faquim-Mauro, Eliana L.
Franzolin, Marcia Regina
Fuchino, Hiroyuki
Mori-Yasumoto, Kanami
Sekita, Setsuko
Kadowaki, Makoto
Satake, Motoyoshi
Konno, Katsuhiro
Resumen
Four novel peptides were isolated from the venoms of the solitary eumenine wasps Eumenes rubrofemoratus and Eumenes fraterculus. Their sequences were determined by MALDI-TOF/TOF (matrix assisted laser desorption/ionization time-of-flight mass spectrometry) analysis, Edman degradation and solid-phase synthesis. Two of them, eumenitin-R (LNLKGLIKKVASLLN) and eumenitin-F (LNLKGLFKKVASLLT), are highly homologous to eumenitin, an antimicrobial peptide from a solitary eumenine wasp, whereas the other two, EMP-ER (FDIMGLIKKVAGAL-NH 2) and EMP-EF (FDVMGIIKKIAGAL-NH 2), are similar to eumenine mastoparan-AF (EMP-AF), a mast cell degranulating peptide from a solitary eumenine wasp. These sequences have the characteristic features of linear cationic cytolytic peptides; rich in hydrophobic and basic amino acids with no disulfide bond, and accordingly, they can be predicted to adopt an amphipathic α-helix secondary structure. In fact, the CD (circular dichroism) spectra of these peptides showed significant α-helical conformation content in the presence of TFE (trifluoroethanol), SDS (sodium dodecylsulfate) and asolectin vesicles. In the biological evaluation, all the peptides exhibited a significant broad-spectrum antimicrobial activity, and moderate mast cell degranulation and leishmanicidal activities, but showed virtually no hemolytic activity. © 2011 Elsevier Ltd.
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