高速AFMカンチレバー

Structural Elucidation of Citric Acid Cross-Linked Pectin and Its Impact on the Properties of Nanocellulose-Reinforced Packaging Films

Citric acid cross-linking is an effective strategy for modifying citrus pectin to enhance its performance in sustainable packaging applications. In this article, Chandra Mohan Chandrasekar, Daniele Carullo, Francesco Saitta, Tommaso Bellesia, Elena Caneva, Chiara Baschieri, Marco Signorelli, Dimitrios Fessas, Stefano Farris and Davide Romano, investigated the structural changes induced by citric acid cross-linking and their influence on the properties of nanocellulose-reinforced packaging films..

The authors demonstrated that cross-linking significantly alters the structure–property relationship of the biopolymer matrix, leading to improved film integrity and modified surface morphology. These results provide valuable insight into biopolymer modification strategies for the development of environmentally friendly packaging materials.

Atomic force microscopy (AFM) was employed to characterize the surface morphology of the films. Measurements were performed using a commercially available AFM instrument operated in contact resonance amplitude imaging (CRAI) mode. A NanoWorld Arrow-FMR AFM probe was used.

This AFM probe features a rectangular beam with a triangular free end and a tetrahedral tip (tip radius ~10 nm, tip height 10–15 μm), with a spring constant of 2.8 N/m and a resonance frequency of 75 kHz. Root mean square surface roughness values were calculated from at least five height-mode images.

Fig. 3. 2D synchronized correlation analysis of FTIR spectra for CLCP packaging film trials. [The intensity of the auto-peaks on the diagonal line represents the overall change in spectral intensity. The key region of interest is the strong auto-peak around 1700 cm−1, highlighted by

Full citation: Chandrasekar, C. M.; Carullo, D.; Saitta, F.; Bellesia, T.; Caneva, E.; Baschieri, C.; Signorelli, M.; Fessas, D.; Farris, S.; Romano, D. “Structural elucidation of citric acid cross-linked pectin and its impact on the properties of nanocellulose-reinforced packaging films.” International Journal of Biological Macromolecules 2025, 333(2), 148869. https://doi.org/10.1016/j.ijbiomac.2025.148869

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Nonlinear Optical Response in Layer-Stacked Gallenene with Ferroelectric Polarization

Layer-stacked gallenene is an emerging two-dimensional material with unique structural and electronic propertiesIn this article, M.Yunusa, A. K.Schulz, T.Parker, et al. investigated the nonlinear optical response of layer-stacked gallenene exhibiting ferroelectric polarization. The material was produced using a liquid metal-based synthesis approach and showed a phase transition associated with its stacked structure.

The authors demonstrated strong second harmonic generation (SHG) signals, revealing the nonlinear optical activity of gallenene and confirming its ferroelectric nature. These findings highlight the potential of gallenene as a novel functional 2D material for advanced optoelectronic and photonic applications.

Atomic force microscopy (AFM) was used to characterize transparent lamellar films and helical filaments. Measurements were performed using a commercially available AFM instrument operated in contact mode. A NanoWorld Arrow-CONTR AFM probe with a nominal force constant of 0.2 N/m and a resonance frequency of 14 kHz was used to obtain high-resolution surface morphology data.

*Figure 1*
Structure of gallenene and complex anatomy of supercooled liquid gallium. Mechanism for electrical and thermal perturbation. a) Illustration of hypothesized interaction of SHG response with SLG in linearly polarized light showing that thermal perturbations could align the 2D nanocrystals, allowing for an increased SHG medium at either temperature or electrical fields. An example HAADF image of gallenene flake sandwiched between two graphene layers, as depicted in (a) (far right microscope image). b) Structural reorganization of gallenene nanocrystals in the SLG leading to an intensity change in SHG signal as a result of thermal or electrical perturbation.

Full citation:

Yunusa, M.; Schulz, A. K.; Parker, T.; Schneider, F.; Elibol, K.; Predel, M.; Dzíbelová, J.; Rebmann, M.; Gorkan, T.; Ye, J.; Tan, J.-C.; Kang, W.; van Aken, P. A.; Meixner, A. J.; Durgun, E.; Kotakoski, J.; Zhang, D.; Sitti, M. Nonlinear Optical Response in Layer-Stacked Gallenene with Ferroelectric Polarization.

Advanced Materials 2025, 37(44), e01058.

https://doi.org/10.1002/adma.202501058

Mechanism for Vipp 1 spiral formation, ring biogenesis, and membrane repair

The ESCRT-III-like protein Vipp1 couples filament polymerization with membrane remodeling. It assembles planar sheets as well as 3D rings and helical polymers, all implicated in mitigating plastid-associated membrane stress. The architecture of Vipp1 planar sheets and helical polymers remains unknown, as do the geometric changes required to transition between polymeric forms. *

In the article “Mechanism for Vipp1 spiral formation, ring biogenesis, and membrane repair” Souvik Naskar, Andrea Merino, Javier Espadas, Jayanti Singh, Aurelien Roux, Adai Colom and Harry H. Low show how cyanobacterial Vipp1 assembles into morphologically-related sheets and spirals on membranes in vitro.*

The spirals converge to form a central ring similar to those described in membrane budding. Cryo-EM structures of helical filaments reveal a close geometric relationship between Vipp1 helical and planar lattices. Moreover, the helical structures reveal how filaments twist—a process required for Vipp1, and likely other ESCRT-III filaments, to transition between planar and 3D architectures. *

Overall, the authors’ results provide a molecular model for Vipp1 ring biogenesis and a mechanism for Vipp1 membrane stabilization and repair, with implications for other ESCRT-III systems. *

NanoWorld Ultra-Short Cantilevers USC-F0.3-k0.3 for High-Speed AFM (HS-AFM) with a typical spring constant of 0.3 N nm−1 and a typical resonance frequency of about 300 kHz were used for image acquisition with fast scanning atomic force microscopy.*

Fig. 2 from Souvik Naskar et al. 2024 “Mechanism for Vipp1 spiral formation, ring biogenesis, and membrane repair”:Vipp1 assembles dynamic networks of spirals, rings and sheets on membrane a, F-AFM phase timecourse showing Vipp1 recruitment to the highly curved edge of membrane patches. Scan rate, 70 Hz; 256 × 256 pixels. The area in the dashed box is enlarged in b. b, Spiral and ring formation localized to the membrane edge. Scan rate, 70 Hz; 256 × 256 pixels. c, Left, phase timecourse showcasing a dense network of sheets, spirals, and rings that ultimately cover the entire membrane plane. Right, average of six F-AFM height images. Scan rate, 120 Hz; 256 × 256 pixels. d, Average F-AFM height image showing Vipp1 sheet, spiral, and ring detail. Red arrows mark the sheet branching into filaments ~13 nm wide. Scan rate, 20 Hz; 256 × 256 pixels. e, Vipp1 sheet and spiral filament height offset from the membrane. f–i, Quantification of Vipp1 filament and spiral characteristics. n = 124, 13, 278, and 278 independent measurements for panels f, g, h, and i, respectively. Error bars show one s.d. of the mean. NanoWorld Ultra-Short Cantilevers USC-F0.3-k0.3-10 with a typical spring constant of 0.3 N nm−1 and a typical resonance frequency of about 300 kHz were used for image acquisition. — Fig. 2 from Souvik Naskar et al. 2024 “Mechanism for Vipp1 spiral formation, ring biogenesis, and membrane repair”:
Vipp1 assembles dynamic networks of spirals, rings and sheets on membrane
a, F-AFM phase timecourse showing Vipp1 recruitment to the highly curved edge of membrane patches. Scan rate, 70 Hz; 256 × 256 pixels. The area in the dashed box is enlarged in b. b, Spiral and ring formation localized to the membrane edge. Scan rate, 70 Hz; 256 × 256 pixels. c, Left, phase timecourse showcasing a dense network of sheets, spirals, and rings that ultimately cover the entire membrane plane. Right, average of six F-AFM height images. Scan rate, 120 Hz; 256 × 256 pixels. d, Average F-AFM height image showing Vipp1 sheet, spiral, and ring detail. Red arrows mark the sheet branching into filaments ~13 nm wide. Scan rate, 20 Hz; 256 × 256 pixels. e, Vipp1 sheet and spiral filament height offset from the membrane. f–i, Quantification of Vipp1 filament and spiral characteristics. n = 124, 13, 278, and 278 independent measurements for panels f, g, h, and i, respectively. Error bars show one s.d. of the mean.

*Souvik Naskar, Andrea Merino, Javier Espadas, Jayanti Singh, Aurelien Roux, Adai Colom and Harry H. Low
Mechanism for Vipp1 spiral formation, ring biogenesis, and membrane repair
Nature Structural & Molecular Biology (2024)
DOI: https://doi.org/10.1038/s41594-024-01401-8

Open Access The article “Mechanism for Vipp1 spiral formation, ring biogenesis, and membrane repair” by Souvik Naskar, Andrea Merino, Javier Espadas, Jayanti Singh, Aurelien Roux, Adai Colom and Harry H. Low is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.