Modeling and simulation of protein–surface interactions: achievements and challenges

M Ozboyaci, DB Kokh, S Corni… - Quarterly reviews of …, 2016 - cambridge.org
Understanding protein–inorganic surface interactions is central to the rational design of new
tools in biomaterial sciences, nanobiotechnology and nanomedicine. Although a significant …

The interplay between carbon nanomaterials and amyloid fibrils in bio-nanotechnology

C Li, R Mezzenga - Nanoscale, 2013 - pubs.rsc.org
Recent advances in bio-nanotechnology have not only rapidly broadened the applications
and scope of hybrid nanomaterials in biological fields, but also greatly enriched the …

Surface effects on aggregation kinetics of amyloidogenic peptides

R Vacha, S Linse, M Lund - Journal of the American Chemical …, 2014 - ACS Publications
The presence of surfaces influences the fibril formation kinetics of peptides and proteins. We
present a systematic study of the aggregation kinetics of amyloidogenic peptides caused by …

The molecular mechanism of fullerene-inhibited aggregation of Alzheimer's β-amyloid peptide fragment

L Xie, Y Luo, D Lin, W Xi, X Yang, G Wei - Nanoscale, 2014 - pubs.rsc.org
Amyloid deposits are implicated in the pathogenesis of many neurodegenerative diseases
such as Alzheimer's disease (AD). The inhibition of β-sheet formation has been considered …

Molecular interactions between graphene and biological molecules

X Zou, S Wei, J Jasensky, M Xiao, Q Wang… - Journal of the …, 2017 - ACS Publications
Applications of graphene have extended into areas of nanobio-technology such as nanobio-
medicine, nanobio-sensing, as well as nanoelectronics with biomolecules. These …

Atomic force microscopy to study molecular mechanisms of amyloid fibril formation and toxicity in Alzheimer's disease

E Drolle, F Hane, B Lee, Z Leonenko - Drug metabolism reviews, 2014 - Taylor & Francis
Alzheimer's disease (AD) is a devastating neurodegenerative disease characterized by
dementia and memory loss for which no cure or effective prevention is currently available …

Chiral effect at protein/graphene interface: a bioinspired perspective to understand amyloid formation

G Qing, S Zhao, Y Xiong, Z Lv, F Jiang… - Journal of the …, 2014 - ACS Publications
Protein misfolding to form amyloid aggregates is the main cause of neurodegenerative
diseases. While it has been widely acknowledged that amyloid formation in vivo is highly …

Interplay between exosomes, microRNAs and toll-like receptors in brain disorders

V Paschon, SH Takada, JM Ikebara, E Sousa… - Molecular …, 2016 - Springer
Extracellular vesicles (EVs), including exosomes, microvesicles and apoptotic bodies,
participate in intercellular communication, and particularly, in paracrine and endocrine …

Nanomaterials for modulating the aggregation of β-amyloid peptides

Y Huang, Y Chang, L Liu, J Wang - Molecules, 2021 - mdpi.com
The aberrant aggregation of amyloid-β (Aβ) peptides in the brain has been recognized as
the major hallmark of Alzheimer's disease (AD). Thus, the inhibition and dissociation of Aβ …

Structure, folding dynamics, and amyloidogenesis of D76N β2-microglobulin: roles of shear flow, hydrophobic surfaces, and α-crystallin

PP Mangione, G Esposito, A Relini, S Raimondi… - Journal of Biological …, 2013 - ASBMB
Systemic amyloidosis is a fatal disease caused by misfolding of native globular proteins,
which then aggregate extracellularly as insoluble fibrils, damaging the structure and function …