Darryl Aucoin

ORCID: 0000-0002-0595-8045
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About
Contact & Profiles
Research Areas
  • Advanced NMR Techniques and Applications
  • Alzheimer's disease research and treatments
  • Protein Structure and Dynamics
  • Supramolecular Self-Assembly in Materials
  • NMR spectroscopy and applications
  • Biochemical effects in animals
  • Computational Drug Discovery Methods
  • Prion Diseases and Protein Misfolding
  • Bone Metabolism and Diseases
  • Graph theory and applications
  • Fuel Cells and Related Materials
  • Lipid Membrane Structure and Behavior
  • Chemical Synthesis and Analysis
  • Electron Spin Resonance Studies
  • Membrane Separation and Gas Transport
  • Trace Elements in Health
  • Polymer crystallization and properties
  • Muon and positron interactions and applications

The Ohio State University
2017-2018

Stony Brook University
2008-2015

College of the Holy Cross
2010

Clark University
2006-2010

Several protein conformational disorders (Parkinson and prion diseases) are linked to aberrant folding of proteins into prefibrillar oligomers amyloid fibrils. Although more toxic than their fibrillar counterparts, it is difficult decouple the origin dissimilar toxicity because fibrils differ both in terms structure size. Here we report characterization two 42-residue β (Aβ42) peptide associated with Alzheimer disease that possess similar size toxicity. We find Aβ42 spontaneously forms at Aβ...

10.1074/jbc.m111.329763 article EN cc-by Journal of Biological Chemistry 2012-05-01

Aβ42 peptides associate into soluble oligomers and protofibrils in the process of forming amyloid fibrils associated with Alzheimer's disease. The have been reported to be more toxic neurons than fibrils, targeted by a wide range small molecule peptide inhibitors. With single touch atomic force microscopy (AFM), we show that monomeric forms two distinct types oligomers, low molecular weight (MW) heights 1-2 nm high MW 3-5 nm. In both cases, are disc-shaped diameters ~10-15 similar suggest...

10.1021/bi500910b article EN publisher-specific-oa Biochemistry 2014-11-25

Soluble oligomers and protofibrils of the Aβ42 peptide are neurotoxic intermediates in conversion monomeric into amyloid fibrils associated with Alzheimer's disease. Nuclear magnetic resonance Fourier transform infrared spectroscopy, along single-touch atomic force microscopy, used to establish structural transitions involved fibril formation. We show that under conditions favorable for nucleated conformation conversion, aggregates largely unstructured low-molecular weight (MW) able stack...

10.1021/acs.biochem.5b00467 article EN Biochemistry 2015-06-12

The pathologic self-assembly of proteins is associated with typically late-onset disorders such as Alzheimer's disease, Parkinson's and type 2 diabetes. Important mechanistic details the are unknown, but there increasing evidence supporting role transient α-helices in early events. Islet amyloid polypeptide (IAPP) a 37-residue that self-assembles into aggregates toxic to insulin-producing β cells. To elucidate events IAPP, we used limited proteolysis identify an exposed flexible region IAPP...

10.1021/ja1069882 article EN Journal of the American Chemical Society 2010-12-07

Abstract One of the most puzzling aspects prion diseases is intricate relationship between strains and interspecies transmissibility barriers. Previously we have shown that certain fundamental mammalian propagation, including strain phenomenon species barriers, can be reproduced in vitro seeded fibrillization Y145Stop protein variant. Here, use solid-state nuclear magnetic resonance spectroscopy to gain atomic level insight into structural differences amyloids from three species: human,...

10.1038/s41467-017-00794-z article EN cc-by Nature Communications 2017-09-25

The assembly and deposition of amyloid β-protein (Aβ) in brain is a key pathological feature Alzheimer’s disease related disorders. Factors have been identified that can either promote or inhibit Aβ brain. We previously reported myelin basic protein (MBP) potent inhibitor fibrillar [Hoos, M. D., et al. (2007) J. Biol. Chem. 282, 9952–9961; Hoos, (2009) Biochemistry 48, 4720–4727]. Moreover, the region on MBP responsible for this activity was localized to 64 N-terminal amino acids (MBP1–64)...

10.1021/bi4001936 article EN Biochemistry 2013-03-19

The structural influence on translational diffusion of 2,2,4-trimethylpentane (TMP) through SEBS triblock polymer (poly(styrene)-block-poly(ethene-co-but-1-ene)-block-poly(styrene)) was studied using pulse field gradient (PFG) NMR coupled with lattice model simulation. Two types PFG experiments were performed: one observing the time-dependent apparent constant and another diffusion-induced signal attenuation. TMP is selectively sorbed into rubbery ethylene/butylenes (EB) phase while glassy...

10.1021/ma062619c article EN Macromolecules 2007-02-10
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