Ayyalusamy Ramamoorthy

ORCID: 0000-0003-1964-1900
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About
Contact & Profiles
Research Areas
  • Advanced NMR Techniques and Applications
  • Alzheimer's disease research and treatments
  • Lipid Membrane Structure and Behavior
  • Solid-state spectroscopy and crystallography
  • NMR spectroscopy and applications
  • Protein Structure and Dynamics
  • Antimicrobial Peptides and Activities
  • Supramolecular Self-Assembly in Materials
  • Electron Spin Resonance Studies
  • Computational Drug Discovery Methods
  • Muon and positron interactions and applications
  • Drug Transport and Resistance Mechanisms
  • Advanced MRI Techniques and Applications
  • Metabolomics and Mass Spectrometry Studies
  • Cholinesterase and Neurodegenerative Diseases
  • Biochemical and Structural Characterization
  • Enzyme Structure and Function
  • Molecular spectroscopy and chirality
  • Pharmacogenetics and Drug Metabolism
  • RNA Interference and Gene Delivery
  • Quantum and electron transport phenomena
  • Spectroscopy and Quantum Chemical Studies
  • Immune Response and Inflammation
  • Mass Spectrometry Techniques and Applications
  • Prion Diseases and Protein Misfolding

Florida State University
2023-2025

University of Michigan
2015-2024

National High Magnetic Field Laboratory
2010-2024

Florida A&M University - Florida State University College of Engineering
2024

Institute of Macromolecular Chemistry
2019-2021

Ann Arbor Center for Independent Living
2012-2020

Arbor Research Collaborative for Health
2020

Weatherford College
2019

Technical University of Munich
2016-2018

Max Planck Computing and Data Facility
2018

Nanoscale building blocks are individually exceptionally strong because they close to ideal, defect-free materials. It is, however, difficult retain the ideal properties in macroscale composites. Bottom-up assembly of a clay/polymer nanocomposite allowed for preparation homogeneous, optically transparent material with planar orientation alumosilicate nanosheets. The stiffness and tensile strength these multilayer composites one order magnitude greater than those analogous nanocomposites at...

10.1126/science.1143176 article EN Science 2007-10-04

LL-37 is an amphipathic, α-helical, antimicrobial peptide. 15N chemical shift and dipolar−shift spectroscopy of site-specifically labeled in oriented lipid bilayers indicate that the amphipathic helix parallel to surface bilayer. This orientation maintained both anionic zwitterionic at different temperatures peptide concentrations, ruling out a barrel-stave mechanism for bilayer disruption by LL-37. In contrast, electrostatic factors, type lipid, presence cholesterol do affect extent which...

10.1021/bi0273563 article EN Biochemistry 2003-05-08

10.1006/jmra.1994.1169 article EN cc-by-nc-nd Journal of Magnetic Resonance Series A 1994-08-01

The aggregation of proteins is tightly controlled in living systems, and misfolded are normally removed before the protein can occur. But for reasons not clearly understood, some individuals this degradation process breaks down, accumulate insoluble aggregates (amyloid deposits) over time. Of many expressed humans, a small but growing number have been found to form long, highly ordered β-sheet fibers that comprise amyloid deposits. Despite lack obvious sequence similarity, forms diverse...

10.1021/ar200189b article EN Accounts of Chemical Research 2011-09-25

Curcumin is the active ingredient of turmeric powder, a natural spice used for generations in traditional medicines. Curcumin's broad spectrum antioxidant, anticarcinogenic, antimutagenic, and anti-inflammatory properties makes it particularly interesting development pharmaceutical compounds. Because curcumin's various effects on function numerous unrelated membrane proteins, has been suggested that affects bilayer itself. However, detailed atomic-level study interaction curcumin with...

10.1021/ja809217u article EN Journal of the American Chemical Society 2009-03-03

Nanoparticles for amyloid diseases: CdTe nanoparticles (NPs) can efficiently prevent fibrillation of peptides; the process is based on multiple binding Aβ oligomers to NPs. The molar efficiency and inhibition mechanism displayed by NPs are analogous found proteins responsible prevention in human body.

10.1002/anie.201007824 article EN Angewandte Chemie International Edition 2011-04-14

The accumulation of metal ions and amyloid-β (Aβ) aggregates found in the brain patients with Alzheimer's disease (AD) has been suggested to be involved AD pathogenesis. To investigate metal-Aβ-associated pathways AD, development chemical tools target metal-Aβ species is desired. Only a few efforts, however, have reported. Here, we report bifunctional small molecules, N-(pyridin-2-ylmethyl)aniline (L2-a) N(1),N(1)-dimethyl-N(4)-(pyridin-2-ylmethyl)benzene-1,4-diamine (L2-b) that can interact...

10.1073/pnas.1006091107 article EN Proceedings of the National Academy of Sciences 2010-12-03

Despite the significance of Alzheimer’s disease, link between metal-associated amyloid-β (metal–Aβ) and disease etiology remains unclear. To elucidate this relationship, chemical tools capable specifically targeting modulating metal–Aβ species are necessary, along with a fundamental understanding their mechanism at molecular level. Herein, we investigated compared interactions reactivities green tea extract, (−)-epigallocatechin-3-gallate [(2 R ,3...

10.1073/pnas.1220326110 article EN Proceedings of the National Academy of Sciences 2013-02-20

LL-37 is a cationic, amphipathic α-helical antimicrobial peptide found in humans that kills cells by disrupting the cell membrane. To disrupt membranes, peptides such as must alter hydrophobic core of bilayer. Differential scanning calorimetry and deuterium (2H) NMR experiments on acyl chain perdeuterated lipids demonstrate inserts into region bilayer alters packing cooperativity. The results show interactions between chains are important for ability this to lipid bilayers its electrostatic...

10.1021/bi036284s article EN Biochemistry 2004-06-12
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