Education & Training
- Doctorate Degree
- Protein Biochemistry - Chosun University, Gwangju, South Korea
Areas of Interests
- Research Interest
- My current research is aimed at developing a sensitive method to detect mosfolded oligomers in biological fluids to be used as possible markers for early diagnosis of neurodegenerative diseases including Alzheimer’s disease (AD) and Parkinson’s disease (PD). Further, to expand the understanding of possible mechanism(s) involved in these diseases and to develop early therapeutic approach, my research also involved the isolation and characterization of toxic aggregates from human AD and PD brains and evaluating their cytotoxic effects in different types of human neurons in vitro.
Dr. Mohammad Shahnawaz received his BSc in Chemistry from Magadh University and MSc in Biochemistry from Jiwaji University in India. He worked as a Junior Unichem Fellow at the National Botanical Research Institute in India. In 2008, he earned his PhD degree in protein Biochemistry from Chosun University in the Republic of Korea. Following this, he worked as a research professor at Chosun University. In 2009, he joined the University of Texas Health Science Center as a post-doctoral fellow and was promoted to instructor position in 2016.
The early diagnosis of neurodegenerative diseases such as Alzheimer’s disease (AD) and Parkinson’s disease (PD) is of utmost importance for the development of disease-modifying or preventive therapies. The central event in AD and PD is misfolding, aggregation and accumulation of amyloid beta peptide (Aβ), Tau and alpha-synuclein (α-Syn) that begins years or decades before the appearance of clinical symptoms. Most importantly, these misfolded oligomers circulate in biological fluids, such as cerebrospinal fluid (CSF) and blood. We have devised a sensitive method to detect tiny amounts of these oligomers present in the biological fluids adapting our Protein Misfolding Cyclic Amplification (PMCA) technology. Using CSF, PMCA amplification of Aβ and α-Syn oligomers allowed us to distinguish AD and PD patients from control individuals affected by other neurodegenerative disorders or nondegenerative neurological diseases. More recently, we have adapted this PMCA technology to detect these oligomers in blood plasma to develop non-invasive diagnostic tests for AD and PD.
Shahnawaz M, Kyung-won Park, Rodrigo Diaz-Espinoza and Soto C. Prion-like Characteristics of the bacterial protein Microcin E492. Scientific Reports. Mar 31; 7:45720, 2017.
Moreno-Gonzalez, I., Edwards, G., Salvadores, N., Shahnawaz, M., Diaz-Espinoza, R. and Soto, C. (2016) Molecular interaction between type 2 diabetes and Alzheimer’s disease through cross-seeding of protein misfolding. Molecular Psychiatry. 2017 Jan 3. doi: 10.1038/mp.2016.230.
Shahnawaz M, Takahiko Tokuda, Masaaki Waragai, Nicolas Mendez, Ryotaro Ishii, Claudia Trenkwalder, Brit Mollenhauer and Claudio Soto. Biochemical diagnosis of Parkinson’s disease by detection of α-synuclein misfolded aggregates in cerebrospinal fluid. JAMA Neurology. 2016 Dec 5. doi: 10.1001/jamaneurol.2016.4547
Salvadores N*, Shahnawaz M*, Scarpini E, Tagliavini F, Soto C. Detection of Misfolded Aβ Oligomers for Sensitive Biochemical Diagnosis of Alzheimer’s Disease. Cell Reports. 2014 Mar 18. pii: S2211-1247(14)00145-4.
Shahnawaz M, Soto Claudio. Microcin amyloid fibrils are a reservoir of toxic oligomeric species. Journal of Biological Chemistry. 2012 Apr 6; 287 (15):11665-76.