Amyloid‐Like Assembly to Form Film at Interfaces: Structural Transformation and Application

Han, Qian; Tao, Fei; Yang, Peng

doi:10.1002/mabi.202300172

Cited by 5 publications

(1 citation statement)

References 105 publications

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“…We conclude by pointing out that the design and synthesis of peptide-based materials with potentially useful applications in technology and biotechnology, driven by amyloid-like cross-β self-assembly, is an active area of current research. − The experimental approaches and results described above are likely to contribute to this field, providing new insights into generic molecular architectures that can underlie such materials.…”

Section: Discussionmentioning

confidence: 97%

Structure of Amyloid Peptide Ribbons Characterized by Electron Microscopy, Atomic Force Microscopy, and Solid-State Nuclear Magnetic Resonance

Thurber,

Yau,

Tycko

2024

J. Phys. Chem. B

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Polypeptides often self-assemble to form amyloid fibrils, which contain cross-β structural motifs and are typically 5− 15 nm in width and micrometers in length. In many cases, short segments of longer amyloid-forming protein or peptide sequences also form cross-β assemblies but with distinctive ribbon-like morphologies that are characterized by a well-defined thickness (on the order of 5 nm) in one lateral dimension and a variable width (typically 10−100 nm) in the other. Here, we use a novel combination of data from solid-state nuclear magnetic resonance (ssNMR), dark-field transmission electron microscopy (TEM), atomic force microscopy (AFM), and cryogenic electron microscopy (cryoEM) to investigate the structures within amyloid ribbons formed by residues 14−23 and residues 11−25 of the Alzheimer's disease-associated amyloid-β peptide (Aβ 14−23 and Aβ 11−25 ). The ssNMR data indicate antiparallel β-sheets with specific registries of intermolecular hydrogen bonds. Mass-per-area values are derived from dark-field TEM data. The ribbon thickness is determined from AFM images. For Aβ 14−23 ribbons, averaged cryoEM images show a periodic spacing of β-sheets. The combined data support structures in which the amyloid ribbon growth direction is the direction of intermolecular hydrogen bonds between β-strands, the ribbon thickness corresponds to the width of one β-sheet (i.e., approximately the length of one molecule), and the variable ribbon width is a variable multiple of the thickness of one β-sheet (i.e., a multiple of the repeat distance in a stack of β-sheets). This architecture for a cross-β assembly may generally exist within amyloid ribbons.

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Section: Discussionmentioning

confidence: 97%

Structure of Amyloid Peptide Ribbons Characterized by Electron Microscopy, Atomic Force Microscopy, and Solid-State Nuclear Magnetic Resonance

Thurber,

Yau,

Tycko

2024

J. Phys. Chem. B

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Amyloid‐based functional materials and their application in flexible sensors

Wu,

Zhang,

et al. 2024

Electron

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Flexible electronic devices have garnered increasing attention for their applications in wearable devices, biomedical systems, soft robots, and flexible displays. However, the current sensors face limitations regarding low sensitivity, poor stability, and inadequate adhesion bonding between stimuli‐responsive functional materials and flexible substrates. To overcome these challenges and enable the further development of sensor devices, surface modification of stimuli‐responsive materials with amyloid aggregates has emerged as a promising approach to enhance functionality and create superior multifunctional sensors. This review presents recent research advancements in the flexible sensors based on protein amyloid aggregation. The article begins by explaining the basic principles of protein amyloid aggregation, followed by outlining the process of preparing 1D to 3D amyloid‐based composite materials. Finally, it discusses the utilization of protein amyloid aggregation as a surface modification technique for developing flexible sensors. Based on this foundation, we identify the shortcomings associated with protein amyloid aggregate composites and propose possible solutions to address them. We believe that comprehensive investigations in this area will expedite the development of high‐performance flexible sensors with high sensitivity, high structural stability, and strong interface adhesion, especially the implantable flexible sensors for health monitoring.

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Recent developments in functional organic polymer coatings for biomedical applications in implanted devices

Yang,

Jia,

Zhao

et al. 2024

Friction

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Organic polymer coatings have been commonly used in biomedical field, which play an important role in achieving biological antifouling, drug delivery, and bacteriostasis. With the continuous development of polymer science, organic polymer coatings can be designed with complex and advanced functions, which is conducive to the construction of biomedical materials with different performances. According to different physical and chemical properties of materials, biomedical organic polymer coating materials are classified into zwitterionic polymers, non-ionic polymers, and biomacromolecules. The strategies of combining coatings with substrates include physical adsorption, chemical grafting, and self-adhesion. Though the coating materials and construction methods are different, many biomedical polymer coatings have been developed to achieve excellent performances, i.e., enhanced lubrication, anti-inflammation, antifouling, antibacterial, drug release, anti-encrustation, anti-thrombosis, etc. Consequently, a large number of biomedical polymer coatings have been used in artificial lungs, ureteral stent, vascular flow diverter, and artificial joints. In this review, we summarize different types, properties, construction methods, biological functions, and clinical applications of biomedical organic polymer coatings, and prospect future direction for development of organic polymer coatings in biomedical field. It is anticipated that this review can be useful for the design and synthesis of functional organic polymer coatings with various biomedical purposes.

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Amyloid‐Like Assembly to Form Film at Interfaces: Structural Transformation and Application

Cited by 5 publications

References 105 publications

Structure of Amyloid Peptide Ribbons Characterized by Electron Microscopy, Atomic Force Microscopy, and Solid-State Nuclear Magnetic Resonance

Structure of Amyloid Peptide Ribbons Characterized by Electron Microscopy, Atomic Force Microscopy, and Solid-State Nuclear Magnetic Resonance

Amyloid‐based functional materials and their application in flexible sensors

Recent developments in functional organic polymer coatings for biomedical applications in implanted devices

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