This study employs (125)I-labeled phytochrome ((125)I-P) from oats to quantitate the binding of phytochrome to a membrane fraction from oats that is highly enriched for mitochondria, and it examines several parameters that influence this attachment. The binding of (125)I-Pfr to the mitochondrial fraction of unirradiated oat seedlings is significantly higher than that of (125)I-Pr. However, (125)I-Pfr and (125)I-Pr bind in equal quantities to mitochondrial preparations isolated from light-exposed seedlings. Maximum (125)I-Pfr binding to membranes from light-exposed plants occurs within 30 seconds and is optimized in a reaction buffer containing 5 millimolar MgCl(2) at pH 6.8. Scatchard plots of the binding data for Pfr indicate a single high-affinity site with an affinity constant of 1.79 x 10(11) per molar. When optimal binding conditions are used, over 20% of the (125)I-P added is bound and a stoichiometry of about 100 molecules per mitochondrion is attained. When the specificity of binding is tested using competition experiments with a 15-fold excess of unlabeled phytochrome, (125)I-Pfr shows no specific binding to rat liver mitochondria.
Download full-text PDF |
Source |
---|---|
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC440706 | PMC |
http://dx.doi.org/10.1104/pp.66.4.696 | DOI Listing |
Am J Trop Med Hyg
January 2025
Centro de Investigaciones Regionales "Dr. Hideyo Noguchi," Universidad Autónoma de Yucatán, Mérida, México.
The socioecological conditions of Mexican regions are conducive to the spread of vector-borne diseases. Although there are established treatment guidelines for dengue and rickettsiosis, diagnosis is complicated. The objective of this work was to identify epitopes of Rickettsia and dengue virus that could be used in serology screening against vector-borne diseases.
View Article and Find Full Text PDFACS Appl Mater Interfaces
January 2025
Department of Microsystems Engineering (IMTEK), Laboratory for Chemistry & Physics of Interfaces (CPI), Albert Ludwigs Universität Freiburg, Georges Köhler Allee 103, 79110 Freiburg, Germany.
Glaucoma, a leading cause of blindness, demands innovative and effective treatments that surpass the limitations of current drug and surgical interventions to lower intraocular pressure. This study describes the generation of cell-repellent hydrogel patches, their deposition on the ocular surface, and a photoinduced chemical binding between the patches and the collagens of the eye. The hydrophilic and protein-repellent hydrogel patch is composed of a copolymer made from dimethylacrylamide and a comonomer unit with anthraquinone moieties.
View Article and Find Full Text PDFJ Med Chem
January 2025
Department of Drug Design and Pharmacology, Faculty of Health and Medical Sciences, University of Copenhagen, Universitetsparken 2, DK-2100 Copenhagen, Denmark.
The Ca/calmodulin-dependent protein kinase II α (CaMKIIα) plays a crucial role in regulating neuronal signaling and higher brain functions, being involved in various brain diseases. Utilization of small molecules targeting the CaMKIIα hub domain has proved to be a promising strategy for specific CaMKIIα modulation and future therapy. Through an structure-based virtual screening campaign, we herein identified 2-arylthiazole-4-carboxylic acids as a new class of high-affinity CaMKIIα hub ligands.
View Article and Find Full Text PDFJ Phys Chem B
January 2025
Department of Chemistry, Indian Institute of Technology Kharagpur, Kharagpur 721302, India.
The microbial aminotransferase enzyme DapC is vital for lysine biosynthesis in various Gram-positive bacteria, including . Characterization of the enzyme's conformational dynamics and identifying the key residues for ligand binding are crucial for the development of effective antimicrobials. This study employs atomistic simulations to explore and categorize the dynamics of DapC in comparison to other classes of aminotransferase.
View Article and Find Full Text PDFJ Med Chem
January 2025
Bioorganic Chemistry Laboratory, New Chemistry Unit, Jawaharlal Nehru Centre for Advanced Scientific Research (JNCASR), Jakkur P.O., Bengaluru 560064, Karnataka, India.
Nucleotide-binding oligomerization domain (NOD)-, leucine-rich repeat (LRR)-, and pyrin domain (PYD)-containing protein 3 (NLRP3) form an inflammasome by assembling with apoptosis-associated speck-like protein containing a CARD (ASC) and procaspase-1 that plays a pivotal role in various neurodegenerative diseases such as Alzheimer's and Parkinson diseases. We designed native peptides derived from the PYDs of NLRP3 and ASC based on their interfacial interaction to inhibit NLRP3 inflammasome formation. Screening revealed that , derived from NLRP3, inhibits inflammasome activation.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!