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Homology modeling and thermostability enhancement of PETase via hydrophobic interactions.
J Biomol Struct Dyn
January 2025
Enzyme and Microbial Technology Research Center, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, Serdang, Selangor, Malaysia.
The quest for sustainable solutions to plastic pollution has driven research into plastic-degrading enzymes, offering promising avenues for polymer recycling applications. However, enzymes derived from natural sources often exhibit suboptimal thermostability, hindering their industrial viability. Protein engineering techniques have emerged as a powerful approach to enhance the desired properties of these biocatalysts.
View Article and Find Full Text PDFProbing the Signal Transduction Mechanism of the Light-Activated Adenylate Cyclase OaPAC Using Unnatural Amino Acid Mutagenesis.
ACS Chem Biol
January 2025
Department of Chemistry, Stony Brook University, Stony Brook, New York 11794-3400, United States.
OaPAC, the photoactivated adenylyl cyclase from , is composed of a blue light using FAD (BLUF) domain fused to an adenylate cyclase (AC) domain. Since both the BLUF and AC domains are part of the same protein, OaPAC is a model for understanding how the ultrafast modulation of the chromophore binding pocket caused by photoexcitation results in the activation of the output domain on the μs-s time scale. In the present work, we use unnatural amino acid mutagenesis to identify specific sites in the protein that are involved in transducing the signal from the FAD binding site to the ATP binding site.
View Article and Find Full Text PDFMEDOC: A Fast, Scalable, and Mathematically Exact Algorithm for the Site-Specific Prediction of the Protonation Degree in Large Disordered Proteins.
J Chem Inf Model
January 2025
Max-Planck-Institut für Immunbiologie und Epigenetik (MPI-IE), Stübeweg 51, 79108 Freiburg im Breisgau, Germany.
Intrinsically disordered regions are found in most eukaryotic proteins and are enriched with positively and negatively charged residues. While it is often convenient to assume that these residues follow their model-compound p values, recent work has shown that local charge effects (charge regulation) can upshift or downshift side chain p values with major consequences for molecular function. Despite this, charge regulation is rarely considered when investigating disordered regions.
View Article and Find Full Text PDFThe periplasmic protein HslJ is the first-line of defense against oxidative stress in Acinetobacter baumannii.
Biol Res
January 2025
Department of Human Sciences and Quality of Life Promotion, San Raffaele University, 00166, Rome, Italy.
Background: Acinetobacter baumannii poses a significant threat globally, causing infections primarily in healthcare settings, with high mortality rates. Its adaptability to antibiotic resistance and tolerance to various stresses, including reactive oxygen species (ROS), contribute to its persistence in healthcare environments. Previous evidence suggested that the periplasmic heat shock protein, HslJ-like protein (ABUW_2868), could be involved in oxidative stress defense in A.
View Article and Find Full Text PDFDesign and in vitro anticancer assessment of a click chemistry-derived dinuclear copper artificial metallo-nuclease.
Nucleic Acids Res
January 2025
School of Chemical Sciences, Dublin City University, Glasnevin, Dublin 9, Ireland.
Copper compounds with artificial metallo-nuclease (AMN) activity are mechanistically unique compared to established metallodrugs. Here, we describe the development of a new dinuclear copper AMN, Cu2-BPL-C6 (BPL-C6 = bis-1,10-phenanthroline-carbon-6), prepared using click chemistry that demonstrates site-specific DNA recognition with low micromolar cleavage activity. The BPL-C6 ligand was designed to force two redox-active copper centres-central for enhancing AMN activity-to bind DNA, via two phenanthroline ligands separated by an aliphatic linker.
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