| Full text | |
| Author(s): Show less - |
Rangel, Marisa
[1]
;
dos Santos Cabrera, Marcia Perez
[2]
;
Kazuma, Kohei
[3]
;
Ando, Kenji
[3]
;
Wang, Xiaoyu
[3]
;
Kato, Manabu
[4]
;
Nihei, Ken-ichi
[5]
;
Hirata, Izaura Yoshico
[6]
;
Cross, Tyra J.
[7]
;
Garcia, Angelica Nunes
[1]
;
Faquim-Mauro, Eliana L.
[1]
;
Franzolin, Marcia Regina
[8]
;
Fuchino, Hiroyuki
[9]
;
Mori-Yasumoto, Kanami
[10]
;
Sekita, Setsuko
[10]
;
Kadowaki, Makoto
[3]
;
Satake, Motoyoshi
[3]
;
Konno, Katsuhiro
[3]
Total Authors: 18
|
| Affiliation: | [1] Butantan Inst, Immunopathol Lab, BR-05503900 Sao Paulo - Brazil
[2] Sao Paulo State Univ, IBILCE, Dept Phys, BR-15054000 Sao Jose Do Rio Preto, SP - Brazil
[3] Toyama Univ, Inst Nat Med, Toyama 9300194 - Japan
[4] Yamada Apiculture Ctr Inc, Okayama 7080393 - Japan
[5] Utsunomiya Univ, Fac Agr, Utsunomiya, Tochigi 3218505 - Japan
[6] Univ Fed Sao Paulo, Dept Biophys, Paulista Med Sch, BR-04044020 Sao Paulo - Brazil
[7] Univ Victoria, Genome BC Prote Ctr, Victoria, BC V8Z 7X8 - Canada
[8] Butantan Inst, Bacteriol Lab, BR-05503900 Sao Paulo - Brazil
[9] Natl Inst Biomed Innovat, Res Ctr Med Plant Resources, Tsukuba, Ibaraki 3050843 - Japan
[10] Tokushima Bunri Univ, Fac Pharmaceut Sci, Kagawa 7692193 - Japan
Total Affiliations: 10
|
| Document type: | Journal article |
| Source: | Toxicon; v. 57, n. 7-8, p. 1081-1092, JUN 2011. |
| Web of Science Citations: | 12 |
| Abstract | |
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 alpha-helix secondary structure. In fact, the CD (circular dichroism) spectra of these peptides showed significant alpha-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. (C) 2011 Elsevier Ltd. All rights reserved. (AU) | |
| FAPESP's process: | 08/00173-4 - Prospection of antimicrobial channel forming natural peptides on cellular membranes and artificial lipid bilayers. |
| Grantee: | Marisa Rangel |
| Support Opportunities: | Regular Research Grants |