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Protein nanotubes (PNTs) as state-of-the-art nanocarriers are promising for various potential applications both in the food and pharmaceutical industries. Derived from edible starting sources like α-lactalbumin, lysozyme, and ovalbumin, PNTs bear properties of biocompatibility and biodegradability. Their large specific surface area and hydrophobic core facilitate chemical modification and loading of bioactive substances, respectively. Moreover, their enhanced permeability and penetration ability across biological barriers such as intestinal mucus, extracellular matrix, and thrombus clot, make it promising platforms for health-related applications. Most importantly, their simple preparation processes enable large-scale production, supporting applications in the biomedical and nanotechnological fields. Understanding the self-assembly principles is crucial for controlling their morphology, size, and shape, and thus provides the ground to a multitude of applications. Here, the current state-of-the-art of PNTs including their building materials, physicochemical properties, and self-assembly mechanisms are comprehensively reviewed. The advantages and limitations, as well as challenges and prospects for their successful applications in biomaterial and pharmaceutical sectors are then discussed and highlighted. Potential cytotoxicity of PNTs and the need of regulations as critical factors for enabling in vivo applications are also highlighted. In the end, a brief summary and future prospects for PNTs as advanced platforms and delivery systems are included.
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http://dx.doi.org/10.1002/adma.202307627 | DOI Listing |
ACS Appl Mater Interfaces
September 2025
Department of Materials Science and Engineering, Gwangju Institute of Science and Technology (GIST), Gwangju 61005, Republic of Korea.
Cyclic peptides (CPs) are versatile building blocks whose conformational constraints foster ordered supramolecular architectures with potential in biomedicine, nanoelectronics, and catalysis. Herein, we report the development of biomimetic antifreeze materials by conjugating CPs bearing ice-binding residues to 4-arm polyethylene glycol (PEG) via click chemistry. The concentration-dependent self-assembly of these CP-PEG conjugates induces programmable morphological transitions, forming nanotube networks above the critical aggregation concentration (CAC) and two-dimensional nanosheet networks near the CAC.
View Article and Find Full Text PDFFront Biosci (Landmark Ed)
August 2025
University of Angers, MitoLab, Unité MITOVASC, UMR CNRS 6015, INSERM U1083, SFR ICAT, 49330 Angers, France.
The bioenergetic machinery of the cell is protected and structured within two layers of mitochondrial membranes. The mitochondrial inner membrane is extremely rich in proteins, including respiratory chain complexes, substrate transport proteins, ion exchangers, and structural fusion proteins. These proteins participate directly or indirectly in shaping the membrane's curvature and facilitating its folding, as well as promoting the formation of nanotubes, and proton-rich pockets known as cristae.
View Article and Find Full Text PDFMikrochim Acta
September 2025
National Research and Development Institute for Chemistry and Petrochemistry ICECHIM, 202 Splaiul Independentei Street, 060021, Bucharest, Romania.
Molecular recognition and determination of vascular cell adhesion molecule-1 (VCAM-1), interleukin-6 (IL-6), and natriuretic peptide C-type (NPPC) are essential for the early prognosis and diagnosis of cardiovascular diseases, especially in young obese populations. Highly sensitive and selective devices characterized by low Limits of quantification are required for their determination in whole blood. Therefore, a 3D stochastic sensor was developed by immobilizing a chitosan hydrogel onto a carbon paste electrode (used as the support matrix for the hydrogel), which was subsequently modified with gold nanoparticles, multi-walled carbon nanotubes, and β-cyclodextrin (β-CD/AuNPs@MWCNT/CS/CPE).
View Article and Find Full Text PDFPhys Chem Chem Phys
September 2025
Department of Physical Chemistry, University of Chemistry and Technology, Technická 5, 16628 Prague, Czech Republic.
In living organisms, proteins and peptides are often under the influence of mechanical forces, especially in confined spaces such as membrane channels, the ribosome exit tunnel, or the proteasome gate. Due to the directional nature of proteins as polymers with distinct ends, forces have the potential to influence protein conformational dynamics in a direction-dependent manner. In this study, we employed force-probe molecular dynamics simulations to investigate the impact of pulling a peptide through a confined environment pushing it in the same direction.
View Article and Find Full Text PDFAdv Mater
September 2025
Departament de Ciència dels Materials i Química Física, Institut de Química Teòrica i Computacional, Universitat de Barcelona, Barcelona, 08028, Spain.
Kelvin probe force microscopy (KPFM) is a highly advanced technique offering notable surface sensitivity and high lateral resolution, ranging from micrometres to the sub-nanometre scale. This scanning probe technique effectively detects local electrical surface potential (ESP), influenced charge distribution, and work function differences, making it essential for studying biological and biochemical processes, from single molecules to complex cellular structures. By enabling nanometre-resolution analysis under simulated conditions, KPFM provides crucial insights into the physicochemical evolution, functionality, and structural organization of biomolecular systems.
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