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Novel peptides from assassin bugs (Hemiptera: Reduviidae): isolation, chemical and biological characterization
Author(s) -
Corzo Gerardo,
Adachi-Akahane Satomi,
Nagao Taku,
Kusui Yoshihisa,
Nakajima Terumi
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02558-3
Subject(s) - chemistry , reduviidae , peptide , hemiptera , circular dichroism , venom , amino acid , high performance liquid chromatography , chromatography , biochemistry , biology , zoology
Three novel peptides were isolated from the venomous saliva of predatory reduviids. They were identified by mass spectrometry and HPLC analysis and consist of 34–36 amino acid residues. They are relatively homologous to the calcium channel blockers ω‐conotoxins from marine cone snails and belong to the four‐loop Cys scaffold structural class. Ptu1, the shortest peptide, was chemically synthesized (sPtu1) and co‐eluted with its native form. Circular dichroism spectra of the sPtu1 showed a high content of β‐turns similar to that of ω‐conotoxins GVIA and MVIIA. Electrophysiological experiments demonstrated that sPtu1 reversibly blocks the N‐type calcium channels expressed in BHK cells.