Detection of Aβ monomers and oligomers: early diagnosis of Alzheimer's disease

Y Zhou, L Liu, Y Hao, M Xu - Chemistry–An Asian Journal, 2016 - Wiley Online Library
Abstract Alzheimer's disease (AD), as the most common progressive neurodegenerative
disorder, is pathologically characterized by deposition of extracellular plaque composed of …

How Single Site Mutations Can Help Understanding Structure Formation of Amyloid β1−40

B Schwarze, D Huster - Macromolecular Bioscience, 2023 - Wiley Online Library
Amyloid fibrils represent the structural endpoint on the energetic (mis) folding landscape of
very many proteins. Physiologically, amyloid fibrils are observed as a characteristic hallmark …

Cell-membrane-mimicking lipid-coated nanoparticles confer Raman enhancement to membrane proteins and reveal membrane-attached amyloid-β conformation

D Bhowmik, KR Mote, CM MacLaughlin, N Biswas… - ACS …, 2015 - ACS Publications
Identifying the structures of membrane bound proteins is critical to understanding their
function in healthy and diseased states. We introduce a surface enhanced Raman …

An early folding contact between Phe19 and Leu34 is critical for amyloid-β oligomer toxicity

AK Das, A Rawat, D Bhowmik, R Pandit… - Acs Chemical …, 2015 - ACS Publications
Small hydrophobic oligomers of aggregation-prone proteins are thought to be generically
toxic. Here we examine this view by perturbing an early folding contact between Phe19 and …

Major reaction coordinates linking transient amyloid-β oligomers to fibrils measured at atomic level

B Chandra, D Bhowmik, BK Maity, KR Mote, D Dhara… - Biophysical …, 2017 - cell.com
The structural underpinnings for the higher toxicity of the oligomeric intermediates of
amyloidogenic peptides, compared to the mature fibrils, remain unknown at present. The …

Altered membrane mechanics provides a receptor‐independent pathway for serotonin action

S Dey, D Surendran, O Engberg… - … A European Journal, 2021 - Wiley Online Library
Serotonin, an important signaling molecule in humans, has an unexpectedly high lipid
membrane affinity. The significance of this finding has evoked considerable speculation …

Ordered and Disordered Segments of Amyloid Beta Drive Sequential Steps of the Toxic Pathway

BK Maity, AK Das, S Dey, UK Moorthi, A Kaur… - Biophysical …, 2019 - cell.com
Pathological amyloid deposits of two intrinsically disordered proteins (IDPs) namely, a-
synuclein (a-syn) and tau, are found in the intracellular Lewy bodies in Parkinson's disease …

A Toxicogenic Interaction between Intracellular Amyloid-β and Apolipoprotein-E

A Dey, A Verma, U Bhaskar, B Sarkar… - ACS Chemical …, 2024 - ACS Publications
Alzheimer's disease (AD) is associated with the aggregation of amyloid β (Aβ) and tau
proteins. Why ApoE variants are significant genetic risk factors remains a major unsolved …

[HTML][HTML] Aggregation-induced conformation changes dictate islet amyloid polypeptide (IAPP) membrane affinity

A Rawat, BK Maity, B Chandra, S Maiti - Biochimica et Biophysica Acta …, 2018 - Elsevier
Islet amyloid polypeptide (IAPP) is a 37 residue intrinsically disordered protein whose
aggregation is associated with Type II diabetes. Like most amyloids, it appears that the …

β-Amyloid peptide interactions with biomimetic membranes: A multiparametric characterization

W Smeralda, M Since, J Cardin, S Corvaisier… - International Journal of …, 2021 - Elsevier
Alzheimer's disease is the most common form of senile dementia in the world, and amyloid β
peptide1-42 (Aβ 1-42) is one of its two principal biological hallmarks. While interactome …