PEGylation is a process in which one or more units of chemically activated polyethylene glycol reacts with a biomolecule, usually a protein, peptide, small molecule or oligonucleotide, creating a putative new molecular entity possessing physicochemical and physiological characteristics that are distinct from its predecessor molecules. In recent years, PEGylation has been used not only as a drug delivery technology but used also as a drug modification technology to transform existing biopharmaceuticals clinically more efficacious than before their PEGylation. PEGylation bestows several useful properties upon the native molecule, resulting in improved pharmacokinetic and pharmacodynamic properties, which in turn enable the native molecule to achieve maximum clinical potency. In addition, PEGylation results in sustained clinical response with minimal dose and less frequency of dosing, leading to improved quality of life via increased patient compliance and reduced cost. During the course of development of various pegylated protein therapeutics, several new insights have been gained. This review article focuses on the approaches, strategies and the utilization of modern PEGylation concepts in the design and development of well-characterized pegylated protein therapeutics.
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http://dx.doi.org/10.1517/17425240802650568 | DOI Listing |
BMC Genomics
January 2025
UCLA Technology Center for Genomics & Bioinformatics, Department of Pathology & Laboratory Medicine, 650 Charles E Young Dr. South, Los Angeles, CA, 90095, USA.
Spatial transcriptomics technology enables the mapping of gene expression within tissues, allowing researchers to visualize the spatial distribution of RNA molecules and gain insights into cellular organization, interactions, and functions in their native environments. A variety of spatial technologies are now commercially available, each offering distinct technical parameters such as cellular resolution, detection sensitivity, gene coverage, and throughput. This wide range of options can make it challenges or create confusion for researchers to select the most appropriate platform for their specific research objectives.
View Article and Find Full Text PDFAnal Chim Acta
February 2025
Department of Chemistry, University of Texas at Austin, Austin, TX, 78712, United States. Electronic address:
Chemical proteomics has advanced small molecule ligand discovery by providing insights into protein-ligand binding mechanism and enabling medicinal chemistry optimization of protein selectivity on a global scale. Mass spectrometry is the predominant analytical method for chemoproteomics, and various approaches have been deployed to investigate and target a rapidly growing number of protein classes and biological systems. Two methods, intact mass analysis (IMA) and top-down proteomics (TDMS), have gained interest in recent years due to advancements in high resolution mass spectrometry instrumentation.
View Article and Find Full Text PDFAnal Chim Acta
February 2025
Regeneron Pharmaceuticals, Inc., Tarrytown, NY, 10591-6707, USA.
Background: The biopharmaceutical industry is increasingly interested in the analysis of trace metals due to their significant impact on product quality and drug safety. Certain metals can potentially accelerate the formation of degradants or aggregates in biotherapeutic proteins, leading to drug product quality concerns. A better understanding of metal-mAb interactions would aid in the development of purification processes and formulations, thereby ensuring better drug quality and safety.
View Article and Find Full Text PDFMetallomics
January 2025
Department of Nutritional Sciences, University of Wisconsin, Madison, WI 53706, USA.
We previously used high pressure liquid chromatography (HPLC) coupled with Se-specific inductively coupled plasma mass spectrometry (ICP-MS) and molecule specific (ESI Orbitrap MS/MS) detection to study the increase in liver Se in turkeys and rats supplemented as selenite in high-Se (5 µg Se/g diet) and adequate-Se diets. We found that far more Se is present as selenosugar (seleno-N-acetyl galactosamine) than is present as selenocysteine (Sec) in true selenoproteins. In high-Se liver, the increase in liver Se was due to low molecular weight (LMW) selenometabolites as glutathione-, cysteine- and methyl-conjugates of the selenosugar, but also as high molecular weight (HMW) species as selenosugars decorating general proteins via mixed-disulfide bonds.
View Article and Find Full Text PDFJ Food Sci
January 2025
School of Life Sciences and Chemistry, Minnan Science and Technology College, Quanzhou, Fujian, China.
Polyphenols are known to interact with starch to form the V-type inclusion complex or the noninclusive complex. It is hypothesized that the addition of polyphenols could improve the properties of Chinese yam (Dioscorea opposita Thunb.) starch, and the properties of the complexes could be regulated by controlling the additive amount of polyphenols.
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