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Among the unique classes of 2D nanomaterials, 2D protein arrays garner increasing attention due to their remarkable structural stability, exceptional physiochemical properties, and tunable electronic and mechanical attributes. The interest in mimicking and surpassing the precise architecture and advanced functionality of natural protein systems drives the field of 2D protein assembly toward the development of sophisticated functional materials. Recent advancements deepen the understanding of the fundamental principles governing 2D protein self-assembly, accelerating the creation of novel functional biomaterials. These developments encompass biological, chemical, and templated strategies, facilitating the self-organization of proteins into highly ordered and intricate 2D patterns. Consequently, these 2D protein arrays create new opportunities for integrating diverse components, from small molecules to nanoparticles, thereby enhancing the performance and versatility of materials in various applications. This review comprehensively assesses the current state of 2D protein nanotechnology, highlighting the latest methodologies for directing protein assembly into precise 2D architectures. The transformative potential of 2D protein assemblies in designing next-generation biomaterials, particularly in areas such as biomedicine, catalysis, photosystems, and membrane filtration is also emphasized.
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http://dx.doi.org/10.1002/advs.202416485 | DOI Listing |
Adv Sci (Weinh)
March 2025
CAS Key Laboratory of Nano-Bio Interface, Division of Nanobiomedicine and i-Lab, Suzhou Institute of Nano-Tech and Nano-Bionics, Chinese Academy of Sciences, Suzhou, 215123, China.
Among the unique classes of 2D nanomaterials, 2D protein arrays garner increasing attention due to their remarkable structural stability, exceptional physiochemical properties, and tunable electronic and mechanical attributes. The interest in mimicking and surpassing the precise architecture and advanced functionality of natural protein systems drives the field of 2D protein assembly toward the development of sophisticated functional materials. Recent advancements deepen the understanding of the fundamental principles governing 2D protein self-assembly, accelerating the creation of novel functional biomaterials.
View Article and Find Full Text PDFCell Genom
March 2025
Institute for Systems Genomics, University of Connecticut, Storrs, CT, USA; Department of Molecular and Cell Biology, University of Connecticut, Storrs, CT, USA; Department of Genetics and Genome Sciences, UConn Health, Farmington, CT, USA. Electronic address:
Great apes have maintained a stable karyotype with few large-scale rearrangements; in contrast, gibbons have undergone a high rate of chromosomal rearrangements coincident with rapid centromere turnover. Here, we characterize fully assembled centromeres in the eastern hoolock gibbon, Hoolock leuconedys (HLE), finding a diverse group of transposable elements (TEs) that differ from the canonical alpha-satellites found across centromeres of other apes. We find that HLE centromeres contain a CpG methylation centromere dip region, providing evidence that this epigenetic feature is conserved in the absence of satellite arrays.
View Article and Find Full Text PDFBMC Microbiol
March 2025
Department of Laboratory Medicine, Fujian Medical University Union Hospital, Fuzhou, 350001, People's Republic of China.
Background: As a quorum sensing system, LuxS/AI-2 is closely associated with bacterial growth, biofilm formation, and virulence. As yet, it is not known how the luxS is associated with a diverse array of physiological activities in non- carbapenemase producing carbapenem resistant Escherichia coli (non-CP-CREC). The purpose of this study is to explore the characterization of AI-2/LuxS quorum sensing system in antibiotic resistance, pathogenicity of non-CP-CREC.
View Article and Find Full Text PDFMetab Eng
March 2025
Shenzhen Maternity and Child Healthcare Hospital, Southern Medical University, Shenzhen, Guangdong, P.R. China. Electronic address:
Aldehydes are ubiquitous metabolites in living cells. As reactive electrophiles, they have the capacity to form adducts with cellular protein thiols and amines, leading to potential toxicity. Dynamic regulation has proven to be an effective strategy for addressing the accumulation of toxic metabolites.
View Article and Find Full Text PDFJ Chromatogr A
March 2025
Analytical Research and Development, MRL, Merck & Co., Inc., 126 E. Lincoln Avenue, Rahway, NJ 07065, USA.
The quantitation of the major capsid protein L1 is an important metric during the pharmaceutical manufacturing of human papilloma virus (HPV) vaccines, as they are critical components of virus like particles (VLPs) that form the core of the drug product. During the production of VLPs, the L1 protein is present in multiple states, including monomer, multimer, fully formed VLPs and aggregate species, whose expression levels provides an important read-out of upstream productivity and downstream purification efficiency through the measurement of step yields. However, quantitation of total L1 protein is challenging not only due to its presence in multiple states, but also due to the matrix complexity and purification stage of the samples, which spans complex cell lysate to cleaner post purification material.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!