alexa Cytolytic and K+ channel blocking activities of beta-KTx and scorpine-like peptides purified from scorpion venoms.
Genetics

Genetics

Single Cell Biology

Author(s): DiegoGarca E, AbdelMottaleb Y, Schwartz EF, de la Vega RC, Tytgat J, , DiegoGarca E, AbdelMottaleb Y, Schwartz EF, de la Vega RC, Tytgat J,

Abstract Share this page

Abstract Among the scorpion venom components whose function are poorly known or even show contrasting pharmacological results are those called "orphan peptides". The most widely distributed are named beta-KTx or scorpine-like peptides. They contain three disulfide bridges with two recognizable domains: a freely moving N-terminal amino acid sequence and a tightly folded C-terminal region with a cysteine-stabilized alpha/beta (CS-alphabeta) motif. Four such peptides and three cloned genes are reported here. They were assayed for their cytolytic, antimicrobial and K (+) channel-blocking activities. Two main characteristics were found: the existence of an unusual structural and functional diversity, whereby the full-length peptide can lyse cells or kill microorganisms, and a C-terminal domain containing the CS-alphabeta motif that can block K (+) channels. Furthermore, sequence analyses and phylogenetic reconstructions are used to discuss the evolution of this type of peptide and to highlight the versatility of the CS-alphabeta structures. This article was published in Cell Mol Life Sci and referenced in Single Cell Biology

Relevant Expert PPTs

Relevant Speaker PPTs

Recommended Conferences

Relevant Topics

Peer Reviewed Journals
 
Make the best use of Scientific Research and information from our 700 + peer reviewed, Open Access Journals
International Conferences 2017-18
 
Meet Inspiring Speakers and Experts at our 3000+ Global Annual Meetings

Contact Us

 
© 2008-2017 OMICS International - Open Access Publisher. Best viewed in Mozilla Firefox | Google Chrome | Above IE 7.0 version
adwords