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Chemical synthesis of a two‐domain scorpion toxin LaIT2 and its single‐domain analogs to elucidate structural factors important for insecticidal and antimicrobial activities
Author(s) -
Juichi Hironori,
Ando Ryo,
Ishido Takafumi,
Miyashita Masahiro,
Nakagawa Yoshiaki,
Miyagawa Hisashi
Publication year - 2018
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.3133
Subject(s) - scorpion toxin , venom , native chemical ligation , peptide , scorpion , antimicrobial peptides , chemistry , toxin , antimicrobial , biochemistry , structure–activity relationship , biological activity , cysteine , scorpion venoms , computational biology , biology , enzyme , in vitro , organic chemistry
Scorpion venom contains various bioactive peptides. Among them, peptides having two different structural domains constitute a toxin family known as β‐KTx or scorpine‐like peptides. These peptides consist of an α‐helical structure in the N‐terminal region and a cysteine‐stabilized structure in the C‐terminal region. This unique structure of β‐KTx peptides contributes to their diverse biological functions, but the importance of each domain for their activities is not fully understood. LaIT2 is a β‐KTx peptide isolated from the venom of the scorpion Liocheles australasiae , which shows both insecticidal and antimicrobial activities. In this study, we chemically synthesized full‐length LaIT2 using a native chemical ligation technique as well as its N‐terminally or C‐terminally truncated single‐domain analogs to evaluate structural factors important for the activities. Biological evaluation of these peptides revealed that the N‐terminal α‐helical domain of LaIT2 is essential for the expression of both insecticidal and antibacterial activities. This suggests that the disruption of membrane structures largely accounts for the biological activities of LaIT2.