Dr. Areej AlHhazmi

Dr.
Areej
AlHhazmi
College of Applied Medical Sciences
Taibah University
Medina, KSA

Fellowship Dates: 

01 January 2020 to 31 December 2020

MIT Department/Faculty Supervisor(s): 

MIT Biology Department, Professor Graham Walker

MIT Fellowship Research Abstract: 

Dr. Areej Alhhazmi's research focuses on two projects, developing an innovative and regulated DNA system to study antimicrobial peptides’ (AMPs) membrane and subcellular actions as well in-depth characterization of an iron sequester/heme binding plant peptide with an antimicrobial activity.

Project 1:

Antimicrobial peptides (AMPs) have great potential to combat antibiotic resistance. AMPs are a subclass of natural peptides, exhibiting broad activity to directly kill bacteria, yeasts, fungi, viruses, and even cancer cells. A single AMP can cause complex physiological responses, not only by perturbing membrane permeability but by interacting with multiple different cellular components as well. The traditional approach of investigating AMPs mechanism of actions by treating bacteria with chemically synthesized AMPs cannot differentiate between the distinctive effects of AMPs on bacterial membranes or intracellular targets in a bacterial cell. Dr. Alhhazmi is working on developing an innovative regulated system in E. coli to investigate the membrane and sub-cellular actions of AMPs.

Project 2:

Alfalfa and Medicago truncatula produce a large family of >600 Nodule Cysteine-Rich (NCR) peptides. These NCRs are not only critically required for bacteroid development and nitrogen fixation process, but for killing internalized bacteria that are not rhizobia, sanctioning non-nitrogen-fixing rhizobia, and killing senescent bacteroids. The smallest member of NCRs is NCR247, composed of 24 amino acids, four of which are cysteines and have broad antimicrobial activity against clinically common pathogens. It has been discovered in Walker’s lab that this cationic peptide was able to sequester iron. Iron is necessary for bacterial metabolism and sequestering iron has an inhibitory effect on bacterial cells. NCR247 was found to be bound to heme with high affinity, rendering the iron inaccessible by making peptide heme complex, uncommon mechanism. Therefore, NCR247 is presented with limitless therapeutically and diagnostic applications. Dr. Alhhazmi is performing in-depth analysis of a collection of different variants of NCR247 related to antimicrobial activity, mammalian cell toxicity, and iron regulated gene expression. 

Professional development 

·       In the process of earning an MIT management Executive education certificate from MIT Sloan of school of management

·       LEAPS program (LEAdership and Professional Strategies and Skills) from School of Science & Physics Department at MIT​

 

Fellowship Sponsored By: 

KACST

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