Elizabeth Nolan

Nolan was born in Niskayuna, New York.[1] She studied at Smith College, where she majored in chemistry and graduated Magna cum Laude in 2000.[1][2] During her undergraduate studies she minored in music and worked with Robert Linck on computational chemistry.[3] She studied the stereoelectronic effects in substituted alkanes.[4] Nolan was a member of Phi Beta Kappa.[1] She was awarded a Fulbright Program Scholarship and moved to France to study siderophore-iron complexes.[2] Nolan moved to Massachusetts Institute of Technology for her graduate studies, where she was supervised by Stephen J. Lippard.[1] She developed small molecule fluorescent sensors to monitor for zinc in neurobiology and mercury in aqueous solutions.[1][5] Together they filed a patent for Fluorescein-based metal sensors.[6] Nolan was a postdoctoral scientist at the Harvard Medical School, working with Christopher T. Walsh on the biosynthetic assembly of microcin E492m.[7] Microcin E492m is an antibiotic peptide that can target Gram-negative bacteria which express siderophore transporters.[1][7] She was awarded a $2.5 million National Institutes of Health grant in 2010 to study antibacterial peptides and zinc in innate immunity.[8] In 2011 she contributed to the book Letters to a Young Chemist.[4][9]

Nolan was appointed as an Assistant Professor at the Department of Chemistry in Massachusetts Institute of Technology in 2014.[1] She explores the coordination chemistry of metal ions in biological systems; in particular how proteins destroy microbes by denying them metal nutrients.[3][10][11] She looks at the peptides and metalloproteins that are involved in mammalian immune response. Her current focus is on calprotectins and how they bind metals.[12][13] She used magnetic circular dichroism to study the binding of iron to human calprotectin.[14] Her group look to understand how Neuronal cells process and removes SOD1 point mutants.[15]

Nolan looks to design drugs to fight bacterial infections.[10] They study how immunity peptides that are encoded by the gene clusters that biosynthesize antibiotics which use metal ion transporters protect the organisms that produce them.[15] She proposes that hijacking the siderophore uptake pathways could allow new prevention and treatment against diseases.[16] She worked with Manuela Raffatellu at University of California, Irvine to develop a new immunisation strategy against salmonella.[17] They target siderophores, a molecule that salmonella secretes to scavenge iron. Immunisation against siderophores led to the production of antibodies that reduced the growth of salmonella and other bacteria.[18] She is on the editorial board of Cell Chemical Biology.[19]