Office: S335, Sackler Sciences Center
Ph.D. Texas A&M University, 1991
M.S. SUNY at Syracuse
B.S. University of the Philippines
Research in the Lazo Lab is focused on the biophysics of misfolding and self-assembly of proteins associated with disease. Proteins of interest include the amyloid β-protein in Alzheimer's disease, islet amyloid polypeptide associated with type 2 diabetes, the prion protein in various forms of prionoses, and skin proteins linked to epidermolysis bullosa, a disease characterized by skin blistering following little or no trauma. A combination of biophysical and biochemical methods including NMR spectroscopy and limited proteolysis/mass spectrometry is used to elucidate the early events of protein misfolding and self-assembly.
Robbins KJ, Liu G, Selmani V, Lazo ND. Conformational analysis of thioflavin T bound to the surface of amyloid fibrils (2012). Langmuir, 28,16490-16495
Liu, G, Gaines JC, Robbins KJ, Lazo ND. Kinetic profile of amyloid formation in the presence of an aromatic inhibitor by nuclear magnetic resonance (2012). ACS Med. Chem Lett. 3, 856-859
Liu G, Robbins KJ, Sparks S, Selmani V, Bilides K, Lazo ND. Helix dipole effects in peptide self-assembly to amyloid (2012). Biochemistry, 51(20): 4167-4174.
Sparks S, Liu G, Robbins KJ, Lazo ND. Curcumin modulates the self-assembly of the islet amyloid polypeptide by disassembling a-helix (2012). Biochem. Biophys. Res. Commun. 422(4): 551-555
Robbins KJ, Lin G, and Lazo ND. Detection of strongly bound thioflavin T species in amyloid fibrils by ligand-detected 1H NMR (2011).J. Phys. Chem. Lett. 2, 735-740
Lui G, Prabhakar A, Aucoin D, Simon M, Sparks S, Robbins KJ, Sheen A, Petty SA, and Lazo ND. Mechanistic studies of peptide self-assembly: Transient α-helices to stable β-sheets (2010). J. Am. Chem. Soc. 132, 18223-18232