Purification and biochemical characterisation of a putative sodium channel agonist secreted from the South African Knobbly sea anemone Bunodosoma capense.
作者： Wynand van Losenoord , Jason Krause , Shirley Parker-Nance , Rui Krause , Stoyan Stoychev
DOI: 10.1016/J.TOXICON.2019.06.222
关键词: Biochemistry 、 Cystine 、 Agonist 、 Bunodosoma 、 Sodium channel 、 Ion channel 、 Peptide 、 Chemistry 、 Tricine 、 Voltage-gated ion channel
摘要: Abstract Voltage gated ion channels have become a subject of investigation as possible pharmaceutical targets. Research has linked the activity directly to anti-inflammatory pathways, energy homeostasis, cancer proliferation and painful diabetic neuropathy. Sea anemones secrete diverse array bioactive compounds including potassium sodium channel toxins. A putative novel agonist (molecular mass 4619.7 Da) with predicted sequence: CLCNSDGPSV RGNTLSGILW LAGCPSGWHN CKKHKPTIGW CCK was isolated from Bunodosoma capense using modified stimulation technique induce secretion neurotoxin rich mucus confirmed by an Artemia nauplii bio-assay. The peptide purification combined size-exclusion reverse-phase high performance liquid chromatography. thallium-based flux assay presence agonist/inhibitor purity determined tricine SDS-PAGE system. indicated multiple disulfide bonds in tight β-defensin cystine conformation. An IC50 value 26 nM for total inhibition on MCF-7 cells. unique initiating bond indicates divergent evolution those previously species.
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