KANMODI RAHMON ILESANMI

Biochemistry

At the Biochemistry department office

Appointment on Visitation important

Topic: CHARACTERIZATION AND PURIFICATION OF CYSTEINE PROTEASE INHIBITOR FROM SEEDS AND FRUITS OF PLANTS

Description:

INTRODUCTION: Cysteine proteases are protein catabolising enzymes. The unwanted and unregulated proteolysis resulting from the activity of cysteine proteases are regulated by Cysteine protease inhibitors (CPIs).  CPI fall under the group of enzymes called Protease Inhibitors (PIs) and are ubiquitously present in plant seeds and fruits.They act by the arresting the negative modulatory activity of cysteine proteases in a number of diseases including diabetes, hypertension, neurodegenerative damages and cancer.

AIM: To isolate, purify and characterise cysteine protease inhibitor from variety of seeds and fruits of plants

Methodology: Ammonium sulphate precipitation, spectrophometry, gel filtration, ion-exchange chromatography and sodium dodecyl polyacrylamide gel electrophoresis (SDS-PAGE).

EXPECTED RESULT: Results are expected to provide information on the mode of inhibition, optimal pH and temperature as well as molecular weight of purified inhibitors.

CONTRIBUTION TO KNOWLEDGE: With a rise in research targeting plant-based bioagents for therapeutic purposes, this research will elucidate and make known plants with attractive cysteine protease inhibitory activity which can be utilised for pharmaceutical applications.

#	Certificate	School	Year
1.	M.Sc (BIOCHEMISTRY)	BIOCHEMISTRY, LAGOS STATE UNIVERSITY, OJO, LAGOS	2019

CHARACTERISATION OF PARTIALLY PURIFIED CYSTEINE PROTEASE INHIBTOR FROM THE SEEDS AND FRUITS OF ANNONA MURICATA

INTRODUCTION: Soursop (Annona muricata) is an edible, lowland tropical fruit-bearing plant that has been widely researched for its source of acetogenin (a potent anticancer agent). However, the precise mechanism responsible for the anticancer activity of acetogenin has not been elucidated. It is therefore imperative to investigate this plant for a different class of anticancer agent. Cysteine proteases inhibitor (CPI) are known to be potent inhibitors of cysteine proteases which are implicated in the pathophysiology of variety of diseases including cancer.

AIM: To purify and characterise cysteine protease from the seeds and fruits of Annona muricata

METHODOLOGY: CPI extracted from the seed and fruit of soursop was isolated and purified by simple methods including ammonium sulphate precipitation, ion-exchange purification and gel filtration. Mode of inhibition, optimal pH and temperature as well effect of metal cation on the activity of the inhibitor was determined by spectrophotometry.

RESULT: Purified CPI from the seed and fruit of soursop displayed competitive and non-competitive inhibition against papain respectively. Maximal inhibitory activity for both seed and fruit samples were observed at similar pH and temperature of 8 and 40⁰C respectively. Although metal cation such as Cu²⁺, Co²⁺ and Zn²⁺ did not effect considerable decrease on the inhibitory activity of the CPI; Pb²⁺, Mn²⁺ and Mg²⁺ significantly inhibited CPI at a very low concentration (1mM)

CONTRIBUTION TO KNOWLEDGE: The antagonistic properties exhibited by the purified CPI from Annona muricata certainly indicate its suitability for pharmaceutical applications in the treatment of some pathological conditions such as cancer and Alzheimer's in which the unwanted proteolysis of cysteine proteases is implicated.

KANMODI RAHMON is a Graduate Assistant at the Department of Biochemistry

KANMODI has a M.Sc in BIOCHEMISTRY from BIOCHEMISTRY, LAGOS STATE UNIVERSITY, OJO, LAGOS