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Kinetic and toxicological effects of synthesized palladium(II) complex on snake venom (Bungarus sindanus) acetylcholinesterase
Ahmed, Mushtaq; Khan, Shahan Zeb; Sher, Naila; Rehman, Zia Ur; Mushtaq, Nadia; Khan, Rahmat Ali.
Affiliation
  • Ahmed, Mushtaq; University of Science and Technology Bannu. Department of Biotechnology. PK
  • Khan, Shahan Zeb; Quaid-i-Azam University. Department of Chemistry. Islamabad. PK
  • Sher, Naila; University of Science and Technology Bannu. Department of Biotechnology. PK
  • Rehman, Zia Ur; Quaid-i-Azam University. Department of Chemistry. Islamabad. PK
  • Mushtaq, Nadia; University of Science and Technology Bannu. Department of Botany. PK
  • Khan, Rahmat Ali; University of Science and Technology Bannu. Department of Biotechnology. PK
J. venom. anim. toxins incl. trop. dis ; J. venom. anim. toxins incl. trop. dis;27: e20200047, 2021. tab, graf
Article в En | VETINDEX, LILACS | ID: biblio-1287090
Ответственная библиотека: BR68.1
ABSTRACT
The venom of the krait (Bungarus sindanus), an Elapidae snake, is highly toxic to humans and contains a great amount of acetylcholinesterase (AChE). The enzyme AChE provokes the hydrolysis of substrate acetylcholine (ACh) in the nervous system and terminates nerve impulse. Different inhibitors inactivate AChE and lead to ACh accumulation and disrupted neurotransmission.

Methods:

The present study was designed to evaluate the effect of palladium(II) complex as antivenom against krait venom AChE using kinetics methods.

Results:

Statistical analysis showed that krait venom AChE inhibition decreases with the increase of Pd(II) complex (0.025-0.05 µM) and exerted 61% inhibition against the AChE at a fixed concentration (0.5 mM) of ACh. Kinetic analysis using the Lineweaver Burk plot showed that Pd(II) caused a competitive inhibition. The compound Pd(II) complex binds at the active site of the enzyme. It was observed that K m (Michaelis-Menten constant of AChE-ACh into AChE and product) increased from 0.108 to 0.310 mM (45.74 to 318.35%) and V max remained constant with an increase of Pd(II) complex concentrations. In AChE K Iapp was found to increase from 0.0912 to 0.025 µM (29.82-72.58%) and did not affect the V maxapp with an increase of ACh from (0.05-1 mM). K i (inhibitory constant) was estimated to be 0.029µM for snake venom; while the K m was estimated to be 0.4 mM. The calculated IC50 for Pd(II) complex was found to be 0.043 µM at constant ACh concentration (0.5 mM).

Conclusions:

The results show that the Pd(II) complex can be deliberated as an inhibitor of AChE.(AU)
Тема - темы
Key words

Полный текст: 1 База данных: LILACS Основная тема: Bungarus / Elapid Venoms / Synthetic Biology Пределы темы: Animals Язык: En Журнал: J. venom. anim. toxins incl. trop. dis Тематика журнала: TOXICOLOGIA Год: 2021 Тип: Article

Полный текст: 1 База данных: LILACS Основная тема: Bungarus / Elapid Venoms / Synthetic Biology Пределы темы: Animals Язык: En Журнал: J. venom. anim. toxins incl. trop. dis Тематика журнала: TOXICOLOGIA Год: 2021 Тип: Article