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David Moffet - Loyola Marymount University. Los Angeles, CA, US

David Moffet

Associate Dean and Professor of Chemistry & Biochemistry | Loyola Marymount University


Seaver College of Science and Engineering





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Phone: 310.338.4400
Email: David.Moffet@lmu.edu
Office: Life Sciences Building 285

Dr. David A. Moffet is a Professor of Chemistry at Loyola Marymount University.

Education (2)

Princeton University: Ph.D., Chemistry 2002

Shippensburg University of Pennsylvania: B.Sc., Chemistry with Biochemistry Concentration 1997

Areas of Expertise (4)

Inorganic Chemistry

Organic Chemistry



Industry Expertise (2)



Research Focus (1)

Preventing the formation of the toxic amyloid linked to Alzheimer’s disease and type 2 diabetes

Several diseases, such as Alzheimer’s disease and type 2 diabetes, are directly linked to the unwanted misfolding of proteins. Rather than being removed by the body, these misfolded proteins aggregate to form a toxic substance called amyloid. The formation of amyloid appears to be directly linked to the progression of these diseases. Our research at LMU involves screening thousands of substances to identify those few that are capable of preventing the formation of toxic amyloid. My students and I have screened through (and continue to screen) hundreds of thousands of substances to identify those that are capable of inhibiting the aggregation of Aβ42 (the amyloid peptide associated with Alzheimer’s disease) and Islet Amyloid Polypeptide (IAPP - the amyloid peptide associated with type 2 diabetes).

Research Grants (1)

Funded Grants

National Institutes of Health 

(1) “Optimizing Peptide Inhibitors of Human IAPP Amyloidogenicity and Identifying Their Effects on the Unfolded Protein Response System” R15 AREA grant 9/12/2019-8/31/2022 Grant#: 1R15DK112172-02 (2) “Investigating the Link Between IAPP Amyloidogenicity and Diabetes Propensity Within the Animal Kingdom” R15 AREA grant 9/20/2016-8/31/2019 Grant#: 1R15DK112172-01 (3) “Inhibition of amyloidogenic Islet Amyloid Polypeptide aggregation with designed combinatorial peptide libraries and small molecules” R15 AREA grant 9/30/2011-8/31/2014 Grant #: 1R15DK094273-01 (4) “Screening of Biological and Synthetic Compounds for the Discovery of Novel Substances that Prevent Amyloid Formation" R15 AREA grant 5/2009-4/2012 Grant #: 1R15AG032582-01A1

Articles (1)

Recent Publications

with LMU undergraduate coauthors

Larry M. Palato, Shannon Pilcher, Alissa Oakes, Arleen Lamba, Jaris Torres, Litza I Ledesma Monjaraz, Crystabel Munoz Edward Njoo, Dillon J. Rinauro, Kate Alexandra Menefee, Angela Tun, Betssy L. Jauregui, Sarah Shapiro, Olivia H. Nossiff, Eileen Olivares, Kevin Chang, Viviane Nguyen, Luiza A Nogaj, and David A Moffet (2019) Amyloidogenicity of Naturally Occurring Full-Length Animal IAPP Variants. J Pept Sci 2019, 25 (8), e3199 Fuentes AF, Hennessy K, Pascual J, Pepe N, Wang I, Santiago A, Chaggan C, Martinez J, Rivera E, Cota P, Cunha C, Nogaj LA, Moffet DA. Identification of plant extracts that inhibit the formation of diabetes-linked IAPP amyloid. J. Herbal Medicine, (2016) 6:37-41. P. Kao, E. Green, C. Pereira, S. Ekimura, D. Juarez, T. Whyte, T. Arhar, B. Malaspina, LA Nogaj, and DA Moffet (2015) Inhibition of toxic IAPP amyloid by extracts of common fruits. J. Functional Foods, 12: 450-457. Bruno E, Catalina P, Roman KP, Takiguchi M, Kao PY, Nogaj LA and Moffet DA (2013) IAPP aggregation and cellular toxicity are inhibited by 1,2,3,4,6-penta-O-galloyl--D-glucose. Amyloid 1: 34-38. Zelus C, Fox A, Calciano A, Faridian BS, Nogaj LA and Moffet DA (2012) Myricetin Inhibits Islet Amyloid Polypeptide (IAPP) Aggregation and Rescues Living Mammalian Cells from IAPP Toxicity. Open Biochemistry Journal 6: 66-70. Neddenriep B, Calciano A, Conti D, Sauve E, Paterson M, Bruno E and Moffet DA (2011) Short Peptides as Inhibitors of Amyloid Aggregation. Open Biotechnology Journal 5: 39-46. Fox A, Snollaerts T, Errecart Casanova C, Calciano A, Nogaj LA and Moffet DA (2010) Selection for Nonamyloidogenic Mutants of Islet Amyloid Polypeptide (IAPP) Identifies an Extended Region for Amyloidogenicity. Biochemistry 49: 7783-7789. Baine M, Georgie D, Shiferraw E, Nguyen T, Nogaj L, and Moffet, D (2009) Inhibition of A 42 aggregation using peptides selected from combinatorial libraries. J. Peptide Science 15, 499-503. Moffet DA (2009) From Gene Mutation to Protein Characterization, Biochem and Mol Biol Ed. 37: 110-115.