Peptide self-assembly: thermodynamics and kinetics

J Wang, K Liu, R Xing, X Yan - Chemical Society Reviews, 2016 - pubs.rsc.org
Self-assembling systems play a significant role in physiological functions and have therefore
attracted tremendous attention due to their great potential for applications in energy …

Self-assembly of peptides: The acceleration by molecular dynamics simulations and machine learning

N Cao, K Huang, J Xie, H Wang, X Shi - Nano Today, 2024 - Elsevier
Peptides, biopolymeric compounds connected by peptide bonds, have garnered significant
attention in recent years as their potential wide applications in fields such as drug delivery …

[HTML][HTML] Self-assembling peptide biomaterials: Insights from spontaneous and enhanced sampling molecular dynamics simulations

BJ Williams-Noonan, A Kamboukos… - Chemical Physics …, 2023 - pubs.aip.org
Peptide self-assembly is the process by which peptide molecules aggregate into low
dimensional (1D, 2D) or 3D ordered materials with potential applications ranging from drug …

β-barrel oligomers as common intermediates of peptides self-assembling into cross-β aggregates

Y Sun, X Ge, Y Xing, B Wang, F Ding - Scientific reports, 2018 - nature.com
Oligomers populated during the early amyloid aggregation process are more toxic than
mature fibrils, but pinpointing the exact toxic species among highly dynamic and …

Expanding the nanoarchitectural diversity through aromatic di-and tri-peptide coassembly: Nanostructures and molecular mechanisms

C Guo, ZA Arnon, R Qi, Q Zhang, L Adler-Abramovich… - ACS …, 2016 - ACS Publications
Molecular self-assembly is pivotal for the formation of ordered nanostructures, yet the
structural diversity obtained by the use of a single type of building block is limited …

Amyloid self‐assembly of hIAPP8‐20 via the accumulation of helical oligomers, α‐helix to β‐sheet transition, and formation of β‐barrel intermediates

Y Sun, A Kakinen, Y Xing, P Faridi, A Nandakumar… - Small, 2019 - Wiley Online Library
The self‐assembly of human islet amyloid polypeptide (hIAPP) into β‐sheet‐rich nanofibrils
is associated with the pathogeny of type 2 diabetes. Soluble hIAPP is intrinsically disordered …

Amphiphilic surface chemistry of fullerenols is necessary for inhibiting the amyloid aggregation of alpha-synuclein NACore

Y Sun, A Kakinen, C Zhang, Y Yang, A Faridi, TP Davis… - Nanoscale, 2019 - pubs.rsc.org
Featuring small sizes, caged structures, low cytotoxicity and the capability to cross biological
barriers, fullerene hydroxy derivatives named fullerenols have been explored as …

[HTML][HTML] Nucleation of β-rich oligomers and β-barrels in the early aggregation of human islet amyloid polypeptide

Y Sun, A Kakinen, Y Xing, EH Pilkington… - … et Biophysica Acta (BBA …, 2019 - Elsevier
The self-assembly of human islet amyloid polypeptide (hIAPP) into β-sheet rich amyloid
aggregates is associated with pancreatic β-cell death in type 2 diabetes (T2D). Prior …

The inhibitory effect of hydroxylated carbon nanotubes on the aggregation of human islet amyloid polypeptide revealed by a combined computational and …

Y Mo, S Brahmachari, J Lei, S Gilead… - ACS chemical …, 2018 - ACS Publications
Fibrillar deposits formed by the aggregation of the human islet amyloid polypeptide (hIAPP)
are the major pathological hallmark of type 2 diabetes mellitus (T2DM). Inhibiting the …

Distinct oligomerization and fibrillization dynamics of amyloid core sequences of amyloid-beta and islet amyloid polypeptide

Y Sun, B Wang, X Ge, F Ding - Physical Chemistry Chemical Physics, 2017 - pubs.rsc.org
A direct observation of amyloid aggregation from isolated peptides to cross-β fibrils is crucial
for understanding the nucleation-dependence process, but the corresponding macroscopic …