Structural, morphological, and kinetic studies of β-amyloid peptide aggregation on self-assembled monolayers
Literature Information
Qiuming Wang, Nilam Shah, Jun Zhao, Chengshan Wang, Chao Zhao, Lingyun Liu, Lingyan Li, Feimeng Zhou, Jie Zheng
The misfolding and aggregation of β-amyloid peptides (Aβ) into amyloid fibrils, a process that has been pathologically linked to the onset of Alzheimer's disease, is dependent on the presence of a heterogeneous surface (e.g., cell membrane). Understanding of the kinetics of amyloid fibril formation and associated structural transition from monomers to intermediates and eventually to fibrils is critical for the development of viable therapeutic agents. In this work, using circular dichroism (CD), atomic force microscopy (AFM), surface plasmon resonance (SPR), and molecular dynamics (MD) simulations, we studied the adsorption, aggregation, and conformational changes of Aβ1–42 from fresh monomers to fully grown fibrils on four model self-assembled monolayers (SAMs): hydrophobic CH3-terminated SAM, hydrophilic OH-terminated SAM, negatively charged COOH-terminated SAMs, and positively charged NH2-terminated SAM. The seeding effect of Aβ1–42 on the kinetics of Aβ aggregation on different SAMs is also examined. The CD, AFM, and SPR data show that all of these SAMs greatly accelerate the formation of β-sheets and amyloid fibrils through surface-enhanced interactions, but Aβ1–42peptides preferentially adsorb on a hydrophobic CH3-SAM and a positively charged NH2-SAM with much stronger interactions than on a hydrophilic OH-SAM and a negatively charged COOH-SAM. MD simulations further reveal that hydrophobic interactions present a general driving force for Aβ adsorption on all SAMs. As Aβ aggregates grow into larger species by packing hydrophobic C-terminals to form a hydrophobic core while exposing hydrophilic and negatively charged N-terminals to solution, electrostatic interactions become more strengthened when they interact with the SAMs especially for the COOH-SAM and the NH2-SAM. Thus, both hydrophobic and electrostatic interactions contribute differently to different Aβ–SAM systems and to different aggregation stages. A postulated mechanism is proposed to describe the structure and kinetics of Aβ aggregation from aqueous solution to the SAMs, providing valuable insights into Aβ aggregation on biological cell membranes.
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Physical Chemistry Chemical Physics (PCCP) is an international journal co-owned by 19 physical chemistry and physics societies from around the world. This journal publishes original, cutting-edge research in physical chemistry, chemical physics and biophysical chemistry. To be suitable for publication in PCCP, articles must include significant innovation and/or insight into physical chemistry; this is the most important criterion that reviewers and Editors will judge against when evaluating submissions. The journal has a broad scope and welcomes contributions spanning experiment, theory, computation and data science. Topical coverage includes spectroscopy, dynamics, kinetics, statistical mechanics, thermodynamics, electrochemistry, catalysis, surface science, quantum mechanics, quantum computing and machine learning. Interdisciplinary research areas such as polymers and soft matter, materials, nanoscience, energy, surfaces/interfaces, and biophysical chemistry are welcomed if they demonstrate significant innovation and/or insight into physical chemistry. Joined experimental/theoretical studies are particularly appreciated when complementary and based on up-to-date approaches.











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