What is the role of lactylation in post-translational modification of proteins?5 answersLactylation, a post-translational modification, plays a crucial role in protein regulation. It involves the addition of lactate to histones and non-histone proteins, impacting gene transcription and protein function. Recent studies have highlighted the significance of lactylation in various biological processes, including cancer, inflammation, and cellular regeneration. The discovery of lactylation on histone lysine residues has expanded our understanding of gene expression regulation. Moreover, lactylation can modulate the activity of proteins like PARP1, showcasing its diverse functional implications. This novel modification not only influences cellular function but also bridges the gap between metabolic reprogramming and epigenetics, offering new insights into the intricate regulatory mechanisms within cells.
How do chemical modifications impact CRISPRi and CRISPRa?10 answersChemical modifications play a crucial role in enhancing the efficiency and specificity of CRISPR interference (CRISPRi) and CRISPR activation (CRISPRa) systems, which are pivotal for gene regulation applications. These modifications can significantly impact the stability, delivery, and off-target effects of CRISPR components, thereby improving their therapeutic potential and research utility.
For CRISPRi and CRISPRa, the guide RNA (gRNA) is a key component whose chemical modification can directly influence the system's performance. Methylation of gRNA, such as m6A and m1A, has been shown to inhibit the DNA cleavage activities of CRISPR-Cas12a by destabilizing the gRNA structure, which prevents the assembly of the Cas12a-gRNA nuclease complex, thus affecting DNA targeting ability. This indicates that specific chemical modifications can be used to regulate the activity of CRISPR systems in a reversible manner, offering a tool for controllable gene editing.
Moreover, the chemical synthesis of modified single-guide RNAs (sgRNAs) through bio-orthogonal chemistry has been developed to efficiently assemble functional sgRNAs containing nucleobase modifications, demonstrating the impact of these modifications on CRISPR activity. This approach highlights the importance of chemical modifications in overcoming the challenges of sgRNA synthesis and enhancing CRISPR system functionality.
Chemical engineering further contributes to the advancement of CRISPR technologies by enabling conditional control of Cas9 activities, improving sgRNA stability and binding affinity, and facilitating nonviral delivery methods. These advancements underscore the significance of chemical modifications in optimizing CRISPR systems for gene therapy and transgenic research.
Additionally, the introduction of protective groups on RNA and the use of amide linkages as nonionic backbone replacements have been explored to conditionally control CRISPR function and improve the stability and specificity of CRISPR-associated RNAs. These chemical strategies enrich the toolbox for CRISPRi and CRISPRa, offering new avenues for precise gene editing and regulation.
In summary, chemical modifications are instrumental in enhancing the performance of CRISPRi and CRISPRa systems by improving gRNA stability, specificity, and delivery, while also providing mechanisms for conditional control and reversible activation of CRISPR functions.
Modification of glycans?5 answersModification of glycans involves altering the structure and properties of polysaccharides and oligosaccharides. Polysaccharides, which are natural macromolecular polymers found in various organisms, can be chemically modified to enhance their biological activities and biomedical applications. Similarly, oligosaccharides, which play important roles in cells and have potential applications in medicine and materials, can be modified to optimize their function and efficacy. Chemoenzymatic approaches have been developed to modify glycan structures on cell surfaces, allowing for the study of glycan-mediated virus infections. In addition, the introduction of selective inhibitors, such as kifunensine, can shift the glycosylation pattern of recombinant proteins from complex-type to oligomannose-type glycans, which can be further modified to produce human-like N-glycan structures. Metabolic engineering and biosynthetic incorporation techniques enable the introduction of reactive functional groups into glycans, providing a means for site-selective modification.
What recent modification food protein?5 answersRecent modifications in food proteins include the use of enzymatically hydrolyzed proteins to impart functional and structural changes in food products. Thermal and non-thermal technologies, such as high-voltage cold plasma, ultrasound, and high-pressure protein, have been explored for protein modification to improve techno-functional properties, digestibility, and allergenicity. Non-thermal processes, including structural transformation and modulation of functional properties, have been found to enhance the digestibility and bioavailability of plant-based proteins. Novel physical processing technologies (NPPT) are being developed to alter protein functionality, reduce anti-nutritional compounds, and prevent damage to heat-labile proteins. Cold plasma treatment has shown promise in improving the solubility, emulsifying, and foaming properties of plant proteins, as well as inactivating antinutritional factors and allergens. These modifications aim to overcome the limitations of plant proteins, such as low solubility and inferior functional properties, to meet the increasing demand for sustainable and healthy plant-based food products.
What is the need of surface modification or coating for protein adsorption?5 answersSurface modification or coating is necessary for protein adsorption because it allows for the control and manipulation of the interaction between biomaterial surfaces and proteins. By modifying the surface properties of biomaterials, such as bioactive glasses (BGs) or silicon dioxide (SiO2), the adsorption of proteins can be enhanced or inhibited, depending on the desired outcome. This is important for various biomedical applications, as protein adsorption plays a crucial role in determining the biocompatibility of biomaterials. Surface engineering techniques, such as treating BGs with different solutions or grafting amino acids onto SiO2 surfaces, can alter the physico-chemical properties of the surfaces, affecting protein adsorption behavior. Understanding and controlling the surface chemistry of materials enables selective improvement of protein adsorption, which is critical for promoting cell attachment and enhancing the biocompatibility of biomaterials.
Amidation enhanced interaction between the modified pectin and the drug, allowing for more efficient drug loading3 answersAmidation of pectin enhanced the interaction between the modified pectin and the drug, resulting in more efficient drug loading. The modified pectin, such as diethonolamine-modified high-methoxyl pectin (DMP) and C12-alkylated pectin (PC12), showed improved drug encapsulation efficiency and sustained drug release behavior. The modified pectin hydrogels exhibited strong interactions with the drug, as indicated by Fourier transform infrared spectroscopy (FTIR) and X-ray diffraction (XRD) studies. These interactions led to increased crystallinity in the hydrogels and improved drug delivery efficiency. The modified pectin hydrogels also demonstrated good water holding properties and compatibility with cells and blood. Overall, amidation of pectin enhanced the interaction between the modified pectin and the drug, allowing for more efficient drug loading and controlled drug release.