Abstract:Lysine acylation plays pivotal roles in cell physiology, including DNA transcription and repair, signal transduction, immune defense, metabolism, and many other key cellular processes. Molecular mechanisms of dysregulated lysine acylation are closely involved in the pathophysiological progress of many human diseases, most notably cancers. In recent years, chemical biology tools have become instrumental in studying the function of post‐translational modifications (PTMs), identifying new “writers”, “erasers” and… Show more
“…This strategy has been widely employed to identify potential binding targets for molecules of interest. 28 , 29 , 30 Figure 3 Development of the chemical probes to investigate lysine lactylation (A) Chemical structure of the p-H4K16laAlk. (B) Proteomic analysis results of p-H4K16laAlk pull down assay (the dotted lines represent p = 0.05 and the enriched ratio = 2).…”
“…This strategy has been widely employed to identify potential binding targets for molecules of interest. 28 , 29 , 30 Figure 3 Development of the chemical probes to investigate lysine lactylation (A) Chemical structure of the p-H4K16laAlk. (B) Proteomic analysis results of p-H4K16laAlk pull down assay (the dotted lines represent p = 0.05 and the enriched ratio = 2).…”
“…Firstly, ultrasonication induces structural changes in the chickpea protein, such as unfolding, denaturation, and fragmentation, which expose more zinc-binding sites and enhance zincprotein interactions [103]. Secondly, succinylation reduces the lysine content in the protein, decreasing competition for zinc binding and allowing more zinc ions to bind to available sites [104]. Tirdly, the ultrasonication process improves protein solubility and accessibility, further promoting zincprotein interactions [104].…”
“…Secondly, succinylation reduces the lysine content in the protein, decreasing competition for zinc binding and allowing more zinc ions to bind to available sites [104]. Tirdly, the ultrasonication process improves protein solubility and accessibility, further promoting zincprotein interactions [104].…”
Zinc is crucial for physiological processes; however, deficiency persists globally. Binding zinc to plant proteins enhances absorption, minimizing toxicity risks and offering a potential solution for deficiency. Mineral binding efficiency of the unmodified protein is limited; hence, dual modification (succinylation and ultrasonication) is potentially used to achieve higher binding efficiency. Enhancing zinc uptake is crucial for cellular health due to its vital roles in various biological processes including enzymatic activity, DNA repair, immune function, antioxidant defense, hormone regulation, brain function, signaling, growth, gene expression, and reproduction. Therefore, this research aimed to develop a chickpea protein-zinc complex and to evaluate the influence of dual modification on their physiochemical, bioavailability, and cellular mineral uptake attributes. Succinylation exhibited significant improvements in the water-holding capacity by 28.73%, oil-holding capacity by 34.09%, and solubility by 5.46% of the chickpea protein-zinc complex as compared to the native complex. Mineral bioavailability increased by 8.32%, and there were notable increases in cellular uptake of zinc by 2.10%, retention by 5.80%, and transport by 3.96%, respectively. Furthermore, the dual modification approach resulted in a notable decrease in the particle size of the chickpea protein-zinc complex, with a substantial reduction of 73.25% and an increased zeta potential value of −21 mV compared to the succinylated complex. As well, dual modification concurrently led to a substantial decline of 48.04% in the sulfhydryl (SH) content, coupled with a marked increase of 21.92% in the surface hydrophobicity. In addition, zinc bioavailability, cellular uptake, retention, and transport were further enhanced by 1.89, 3.34, and 4.8% through dual modification. Our findings highlight that the dual modification of the chickpea protein-zinc complex shows a promising strategy for enhancing the techno-functional characteristics, bioavailability, and cellular uptake of zinc, which could be a better platform for developing vegan foods.
Multiplex detection of protein post-translational modifications (PTMs), especially at point-of-care, is of great significance in cancer diagnosis. Herein, we report a machine learning-assisted photonic crystal hydrogel (PCH) sensor for multiplex detection of PTMs. With closely-related PCH sensors microfabricated on a single chip, our design achieved not only rapid screening of PTMs at specific protein sites by using only naked eyes/cellphone, but also the feasibility of real-time monitoring of phosphorylation reactions. By taking advantage of multiplex sensor chips and a neural network algorithm, accurate prediction of PTMs by both their types and concentrations was enabled. This approach was ultimately used to detect and differentiate up/down regulation of different phosphorylation sites within the same protein in live mammalian cells. Our developed method thus holds potential for POC identification of various PTMs in early-stage diagnosis of protein-related diseases.
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