A polyelectrolyte multilayer (PEM) system based on biopolymers has been constructed and studied in its formation and enzymatic breakdown. The multilayer is composed of fucoidan (a proven antimicrobial/anti-inflammatory seaweed-based polysaccharide) and poly-l-arginine (a polypeptide that can be readily degraded with trypsin to yield arginine, a known NO donor), thus making the multilayer a potential dual action surface treatment for wound dressings. Studies on the formation of the multilayer revealed that the film built-up in the expected stepwise manner with consistent reversal of the zeta potential upon the adsorption of each subsequent polyion. The completed film (8 bilayers) was seen to have low hydration (30% water), as determined by HO/DO solvent replacement studies using the quartz crystal microbalance, with an adsorbed mass (without hydration water) of approx. 4.8μgcm, as determined by quantitative attenuated total reflectance Fourier transform infrared (ATR FTIR) spectroscopy. The enzymatic breakdown of the film in response to exposure to trypsin was also investigated, and the film was seen to release both polymers over time, with a projected complete film removal period of approximately 24h. Critically, this information was determined using ATR FTIR spectroscopy experiments, which allowed unambiguous deconvolution of the removal rates of the two polyions, which is information that cannot be obtained from other methodologies used to study enzymatic breakdown of surface films.
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http://dx.doi.org/10.1016/j.colsurfb.2017.08.005 | DOI Listing |
ACS Synth Biol
January 2025
Centre for Engineering Biology, Institute of Quantitative Biology, Biochemistry and Biotechnology, School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3FF, U.K.
The "Protein synthesis Using Recombinant Elements" ("PURE") system is a minimal biochemical system capable of carrying out cell-free protein synthesis using defined enzymatic components. This study extends PURE by integrating an ATP regeneration system based on pyruvate oxidase, acetate kinase, and catalase. The new pathway generates acetyl phosphate from pyruvate, phosphate, and oxygen, which is used to rephosphorylate ATP .
View Article and Find Full Text PDFAnal Bioanal Chem
January 2025
Institute of Inorganic and Analytical Chemistry, University of Münster, Münster, Germany.
Tattooing is a popular form of body art that has evolved from ancient times into being part of modern society. The understanding of biotransformation processes of coloring tattoo pigments in human skin is limited although skin reactions to tattoos with unknown culprits occur. Electrochemistry coupled to mass spectrometry (EC-MS) has widely been used as a tool for a purely instrumental approach to simulating the enzymatic biotransformation of xenobiotics.
View Article and Find Full Text PDFInt J Biol Macromol
January 2025
School of Basic Medicine, Qingdao University, Qingdao 266071, China. Electronic address:
Fructose-1,6-bisphosphatase 1 (FBP1) is a key gluconeogenic enzyme that plays complex and context-dependent roles in cancer biology. This review comprehensively examines FBP1's dual functions as both a tumor suppressor and an oncogene across various cancer types. In many cancers, such as hepatocellular carcinoma, clear cell renal cell carcinoma, and lung cancer, downregulation of FBP1 contributes to tumor progression through metabolic reprogramming, promoting glycolysis, and altering the tumor microenvironment.
View Article and Find Full Text PDFProc Natl Acad Sci U S A
January 2025
Department of Chemistry and Biochemistry, The University of Texas at Dallas, Richardson, TX 75080.
Alzheimers Dement
December 2024
University of Texas Southwestern Medical Center, Dallas, TX, USA.
Background: The prion model of tau propagation in Alzheimer's Disease predicts that tau seeds are released from cells and taken up by neighboring cells, resulting in spreading of the disease. Our previous work revealed that tau aggregates bind to heparan sulfate proteoglycans (HSPGs) on the cell surface, followed by cellular uptake via macropinocytosis. HSPGs are glycoproteins, consisting of a protein core and decorated with linear glycosaminoglycan (GAG) chains called heparan sulfate (HS) with highly variable sulfation patterns.
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