The continuous production and widespread applications of synthetic plastics and their waste present immense environmental challenges and damage living systems. Microplastics (MPs) have become of great concern in various ecosystems due to their high stability and decomposition into smaller fragments such as nano-plastics (NPs). Nevertheless, MPs and NPs can be removed from the environment using several physical, chemical, and microbiological methods. This study presents a comprehensive narrative literature review, which aims to explore the various types of MPs and NPs, their sources, fate, toxicity, and impact on human health and environment. To achieve this aim, the study employed a comprehensive literature review methodology. In addition, it summarizes various methods of sample collection and analysis techniques. Remediation strategies for MPs and NPs removal are assessed and compared. Furthermore, it highlights interlinkages between the sustainable development goals (SDGs)—specifically SDG 14—and plastic pollution. Overall, priority for research and development in the field of MPs and NPs impacts on ecological ecosystems is a must as this will enable the development of scientific polices driven by global collaboration and governance which in turn will develop tools and methodologies that measure the impacts and risk of plastic pollution.
X-ray crystallography is a robust and powerful structural biology technique that provides high-resolution atomic structures of biomacromolecules. Scientists use this technique to unravel mechanistic and structural details of biological macromolecules (e.g., proteins, nucleic acids, protein complexes, protein-nucleic acid complexes, or large biological compartments). Since its inception, single-crystal cryocrystallography has never been performed in Türkiye due to the lack of a single-crystal X-ray diffractometer. The X-ray diffraction facility recently established at the University of Health Sciences, İstanbul, Türkiye will enable Turkish and international researchers to easily perform high-resolution structural analysis of biomacromolecules from single crystals. Here, we describe the technical and practical outlook of a state-of-the-art home-source X-ray, using lysozyme as a model protein. The methods and practice described in this article can be applied to any biological sample for structural studies. Therefore, this article will be a valuable practical guide from sample preparation to data analysis.
Gold nanoparticles (AuNPs) can cross the blood brain barrier, thus can be used as nanocarriers in brain drug delivery. However, the effect of bare and polyethylene glycol-modified (PEGylated) AuNPs on normal neural function has not been extensively investigated. In this study, bioelectrical properties of neuronal functions of male BALB/c mice were explored ex vivo and in vivo by using 5 nm bare AuNPs and PEGylated AuNPs. Electrophysiological properties of neurons from hippocampal CA1 region sections were recorded by patch clamp method. Ex vivo, firing rate of action and membrane potentials in response to negative current stimuli significantly altered only after bare AuNP exposure compared to control (p < 0.05). After in vivo injections, anxiety levels of animals were similar. Amplitude of action potentials reduced only in bare AuNP group (p < 0.05). In conclusion, excitability of hippocampal neurons is increasing with bare AuNP exposure, and PEGylation might be more biocompatible for medical applications.
6 May 2025 in Journal of Photochemistry and Photobiology A: Chemistry
X-ray crystallography is a robust and powerful structural biology technique that provides high-resolution atomic structures of biomacromolecules. Scientists use this technique to unravel mechanistic and structural details of biological macromolecules (e.g. proteins, nucleic acids, protein complexes, protein-nucleic acid complexes, or large biological compartments). Since its inception, single-crystal cryo-crystallography has never been performed in Türkiye due to the lack of a single-crystal X-ray diffractometer. The X-ray diffraction facility recently established at the University of Health Sciences, Istanbul, Türkiye will enable Turkish and international researchers to easily perform high-resolution structural analysis of biomacromolecules from single crystals. Here, we describe the technical and practical outlook of a state-of-the-art home-source X-ray, using lysozyme as a model protein. The methods and practice described in this article can be applied to any biological sample for structural studies. Therefore, this article will be a valuable practical guide from sample preparation to data analysis.