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We conducted molecular dynamics simulations to investigate chain conformations in adsorbed layers during polymer capillary imbibition. While the imbibition length adheres to the classical Lucas-Washburn equation, a notable deviation in mobile bead density emerges under strong confinement, consistent with in situ dielectric spectroscopy experiments. The proportion of loop structures within adsorbed layers progressively increases during capillary infiltration, attributed to the relaxation of initially stretched chains toward equilibrium configurations. Furthermore, systematic analysis revealed that chain relaxation dynamics exhibit length-dependent retardation, especially under high confinement. The characteristic desorption time demonstrates chain-length dependence in quantitative agreement with scaling predictions.
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http://dx.doi.org/10.1063/5.0270676 | DOI Listing |
Spectrochim Acta A Mol Biomol Spectrosc
September 2025
College of Chemistry, Zhengzhou University, Zhengzhou, Henan 450001, PR China.
The interactions of three berberine mid-chain fatty acid salts ([BBR][C], n = 6, 7, 8) with lysozyme (Lyz) are investigated in detail using multi-spectroscopic and molecular docking techniques. Steady-state fluorescence and UV-visible absorption experiments suggest that the binding mechanism of [BBR][C] on Lyz is a static quenching with a binding ratio of 1:1. The compound [BBR][C] exhibits a moderate binding affinity toward Lyz.
View Article and Find Full Text PDFACS Appl Mater Interfaces
September 2025
Department of Materials Science and Engineering, Iowa State University, Ames, Iowa 50011, United States.
Distinctive polymer brushes (PBs) play a crucial role in providing a nonpreferential (neutral) surface for vertical orientation of block copolymers (BCPs). This bottom-up approach effectively aligns the formation of vertical lamellar and cylinder lattice structures from the BCP, which is crucial for nanopatterning and other applications. In conventional BCP self-assembly techniques, random copolymer brushes are commonly employed to achieve substrate neutrality.
View Article and Find Full Text PDFMAbs
December 2025
Office of Pharmaceutical Quality Research, Office of Pharmaceutical Quality, Center for Drug Evaluation and Research, Food and Drug Administration, Silver Spring, MD, USA.
The analytical comparability of biologic products and their biosimilars, including higher-order structure (HOS) assessment, ensures product quality and is required for regulatory approval. In this study, nuclear magnetic resonance (NMR) spectroscopy was used to evaluate the HOS of Humira (adalimumab) and its biosimilars under normal and photo-stressed conditions. Under normal conditions, 1D and 2D NMR spectra showed strong structural similarity among all products.
View Article and Find Full Text PDFSpectrochim Acta A Mol Biomol Spectrosc
September 2025
Changchun Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Changchun 130122, China. Electronic address:
To achieve ultrasensitive and real-time detection of the H1N1 influenza virus, this study designed a nucleic acid-free fluorescent biosensor based on 3D spherical DNA nanostructure and CRISPR/Cas12a (3D-SDNC). The biosensor constructs a rigid 3D nano-framework via self-assembly of six oligonucleotide chains, with H1N1-specific nucleic acid aptamers and Cas12a activator strands strategically positioned at multi-spined vertices for precise spatial coupling between viral recognition and signal transduction. Upon aptamer-virus binding, the induced conformational change liberates the activator strand, thereby activating the trans-cleavage activity of the Cas12a/crRNA complex to efficiently cleave the HEX/BHQ1 double-labeled fluorescent probe and initiate cascade signal amplification.
View Article and Find Full Text PDFIEEE Trans Comput Biol Bioinform
September 2025
Deciphering the three-dimensional structure of proteins remains a grand challenge in biology and medicine, as it holds the key to understanding their biological functions and facilitating drug discovery. In this paper, we introduce DECIPHER (Deep Encoding of Cellular Interactions and Protein HiErarchical Representation), a novel deep graph learning framework for protein structure prediction. By representing proteins as graphs, where residues and atoms serve as nodes and their interactions form edges, we capture the intricate spatial relationships within these complex biomolecules.
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