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 …
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 …
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 …
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 …
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 …
Featuring small sizes, caged structures, low cytotoxicity and the capability to cross biological barriers, fullerene hydroxy derivatives named fullerenols have been explored as …
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 …
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 …
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 …