Andrei Alexandrescu


Molecular and Cell Biology / Structural Biology, Biochemistry and Biophysics (SB3)

Education: Ph.D. University of Wisconsin-Madison; Postdoctoral study, Oxford University; Johns Hopkins University Medical Institutes

Research Interests: High-resolution solution NMR investigations of protein structure, folding, dynamics, and association;
Amyloid fibrils: Amylin (type 2 diabetes), A-beta (Alzheimer’s Disease), alpha-synuclein (Parkinson’s Disease), SEVI (HIV infectivity);
Protein folding intermediates, protein structure conservation, and evolution of protein structure; Accessory domain modules of virus coat proteins and bacterial pathogens.

Selected Publications:
[Click here to get nearly full publication list.]

Dedeo, C.L., Teschke, C.M., & Alexandrescu, A.T(2020) “Keeping it together: structures, functions, and applications of viral decoration proteins”, Viruses 12, 1163.

Whitehead, R. D. III, Teschke, C.M., & Alexandrescu, A.T (2019) “NMR mapping of disordered segments for a viral scaffolding protein enclosed in a 23 MDa procapsid”, Biophysical J., in press,

Newcomer, R.L., Schrad, J.R., Gilcrease, E.B., Casjens, S.R., Feig, M., Teschke, C.M., Alexandrescu, A.T, & Parent K.N. (2019) “The phage L capsid decoration protein has a novel OB-fold and an unusual capsid binding strategy”, eLife 8, e45345.

Tripler, T.N., Kaplan, A.R., Alexandrescu, A.T, & Teschke, C.M. (2019) “Conservation and divergence of the I-domain inserted into the ubiquitous HK97 coat protein fold in the P22-like bacteriophages”, Journal of Virology, in press

Newcomer, R.L., Belato, H.B., Teschke, C.M. & Alexandrescu, A.T (2018) “NMR assignments for monomeric phage L decoration protein”, Biomolecular NMR Assignments 12, 339-343

Asthana, S., Mallick, B., Alexandrescu, A.T & Jha, S. (2017) “IAPP in type II diabetes: Basic research on structure, molecular interactions, and disease mechanisms suggests potential intervention strategies”, BBA Biomembranes (Special Issue on Protein Aggregation), [Epub ahead of print]

Anne R Kaplan, Katherine Kaus, Swastik De, Rich Olson & Andrei T Alexandrescu (2017) “NMR structure of the Bacillus cereus hemolysin II C-terminal domain reveals a novel fold.” Scientific Reports 7: 3277, DOI:

Anne R Kaplan, Megan R Brady, Mark W Maciejewski, Richard A Kammerer & Andrei T Alexandrescu (2017) “NMR Structures of GCN4p are Largely Conserved when Ion Pairs are Disrupted at Acidic pH but Show a Relaxation of the Coiled Coil Superhelix.” Biochemistry, 56, 1604-1619 , DOI: 10.1021/acs.biochem.6b00634 [Epub ahead of print]

Christina Harprecht, Oghenfejiro Okifo, Kevin J. Robbins, Tina Motwani, Andrei T. Alexandrescu & Carolyn M. Teschke (2016) “Contextual role of a salt-bridge in the phage P22 coat protein I-domain.” J. Biol. Chem.  291, 11359-11372.

Newcomer, R.L., Fraser, L.C.R., Teschke, C.M. & Alexandrescu, A.T. (2015) “Mechanism of protein denaturation: partial unfolding of the P22 coat protein I-domain by urea binding.”, Biophysical J. 109, 2666-2677. doi: 10.1016/j.bpj.2015.11.010

Alexandrescu, A.T. (2016) “Quenched Hydrogen Exchange NMR of Amyloid Fibrils.” Methods in Mol. Biol. 1345, 211-222. doi: 10.1007/978-1-4939-2978-8_14

Tripler, T.N., Maciejewski, M.W., Teschke, C.M. & Alexandrescu, A.T. (2015) “NMR assignments for the insertion domain of bacteriophage CUS-3 coat protein.” Biomolecular NMR Assignments 9, 333-336. doi: 10.1007/s12104-015-9604-4

Patil S.M., & Alexandrescu, A.T. (2015) “Charge-based inhibitors of amylin fibrillization and toxicity.” J. Diabetes Res., Article ID 946037.

Rizzo, A.A., Suhanovsky, M.M., Baker, M.L., Fraser, L.C.R., Jones, L.M., Rempel, D.L., Gross, M.L., Chiu, W., Alexandrescu, A.T. & Teschke, C.M. (2014) “Multiple functional roles of the accessory I-domain of bacteriophage P22 coat protein revealed by NMR structure and cryoEM modeling”. Structure 22, 830-841.

Jha, S., Snell, J.M., Sheftic, S.R., Patil S.M., Daniels, S.B., Kolling, F.W., & Alexandrescu, A.T. (2014) “pH dependence of amylin fibrillization”. Biochemistry 53, 300-310. DOI: 10.1021/bi401164k

Sheftic, S.R., White, E., Gage, D.J. & Alexandrescu, A.T. (2014) “NMR structure of the HWE kinase associated response regulator Sma0114 in its activated state”. Biochemistry 53, 311-322. DOI: 10.1021/bi401497h

Anne R. Kaplan, Mark W. Maciejewski, Rich Olson, Andrei T. Alexandrescu (2014). NMR assignments for the cis and transforms of the hemolysin II C-terminal domain. Biomol NMR Assign 8, 419-423 [Epub ahead of print] . doi: 10.1007/s12104-013-9530-2

Alexandrescu, A.T. (2013) “Amide proton solvent protection in amylin fibrils probed by quenched hydrogen exchange NMR”. PLoS One, e56467. doi: 10.1371/journal.pone.0056467

Sheftic, S.R., Garcia, P.P., White, E., Robinson, V.L., Gage, D. & Alexandrescu, A.T. (2012) “Nuclear Magnetic Resonance Structure and Dynamics of the Response Regulator Sma0114 from Sinorhizobium meliloti”. Biochemistry 51, 6932-6941.

Sheftic, S.R., Snell, J. M., Jha, S. & Alexandrescu, A.T. (2012) “Inhibition of Semen-derived Enhancer of Virus Infection (SEVI) fibrillogenesis by physiological zinc and copper concentrations”, European Biophysics Journal 41, 695-704. DOI: 10.1007/s00249-012-0846-0

Jha, S., Patil, S.M., Gibson, J., Nelson, C.E., Alder, N.N., Alexandrescu, A.T. (2011) “Mechanism of amylin fibrillization enhancement by heparin”. J. Biol. Chem. 286, 22894-22904. doi:10.1074/jbc.M110.215814

Patil, S.M., Mehta, A., Jha, S. & Alexandrescu, A.T (2011) “Heterogeneous amylin fibril growth mechanisms imaged by Total Internal Reflection Fluorescence Microscopy”. Biochemistry 50, 2808-2819. DOI: 10.1021/bi101908m

Andre Alexandrescu
Contact Information
Mailing Address91 North Eagleville Road, Unit 3125, Storrs, CT 06269-3125
Office LocationBiology/Physics Building 209