Proteomic analysis of two novel peptides from the Odontobuthus doriae scorpion venom

被引：0
|
作者：
Zargan, Jamil [1 ]
Jahangirian, Ehsan [1 ]
Khan, Haider A. [2 ]
Ali, Shakir [3 ]
机构：
[1] Imam Hossein Univ, Fac Basic Sci, Dept Biol, Nanobiotechnol, Tehran 1698715461, Iran
[2] Hamdard Univ, Dept Med Elementol & Toxicol, Jamia Hamdard, New Delhi 110062, India
[3] Hamdard Univ, Dept Biochem, Jamia Hamdard, New Delhi 110062, India
来源：
JOURNAL OF ASIAN NATURAL PRODUCTS RESEARCH | 2025年 / 27卷 / 03期
关键词：
Odontobuthus doriae; MALDI-TOF/MS; scorpion venom; proteomic; peptide; LEUKEMIA-CELL LINE; MOLECULAR CHARACTERIZATION; SELECTIVE TOXIN; PROTEINS; PURIFICATION; APOPTOSIS; CHLOROTOXIN; COMPONENTS; FRACTIONS; CHANNELS;
D O I：
10.1080/10286020.2024.2403612
中图分类号：
Q94 [植物学];
学科分类号：
071001 ;
摘要：
The venom of the Odontobuthus doriae scorpion, prevalent in East Asia and Iran, has not been fully characterized. This study provides the first proteomic profile of O. doriae venom to explore its potential as a medical. 2D-PAGE analysis revealed 96 protein spots with isoelectric points from 3 to 9 and molecular weights between 6.6 to 205 kDa. Fourteen toxin fractions were isolated via HPLC, and SDS-PAGE showed seven protein bands ranging from 3.8 to 182 kDa. MALDI-TOF MS identified Peptide 1 and Peptide 2, resembling Hemoglobin beta-2 chain and Chaperonin HSP60 and suggest potential therapeutic applications for P1 and P2.
引用
收藏
页码：301 / 322
页数：22
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