Hesperidin (HE), a significant flavonoid polyphenolic compound present in citrus plants, exhibits diverse pharmacological effects. Considering the crucial involvement of biological membranes and transporter proteins in the transportation and biological processes of HE, it becomes essential to comprehend the potential mechanisms through which HE interacts with membranes and transporter proteins. In order to simulate the process of active molecule transport, a cell membrane model consisting of 1,2-dipalmitoyl-n-glycero-3-phosphatidylcholine (DPPC) and a transporter protein model of bovine serum albumin (BSA) were employed for investigation. The present study aimed to investigate the mechanism of action of hesperidin (HE) in DPPC and BSA using fluorescence quenching, Fourier transform infrared spectroscopy (FTIR), and differential scanning calorimetry (DSC). The localization and interaction of HE within liposomes were also elucidated. Furthermore, the binding of BSA and HE was analyzed through UV/Vis absorption spectroscopy, fluorescence spectroscopy, infrared spectroscopy, and computational biology techniques. Computational biology analysis revealed that the binding between HE and BSA primarily occurred via hydrogen bonding and hydrophobic interactions. This study aimed to investigate the role and mechanism of HE in the DPPC cell membrane model and the BSA transporter protein model, thereby offering novel insights into the action of HE in DPPC and BSA.
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http://dx.doi.org/10.1016/j.saa.2024.124172 | DOI Listing |
BMC Chem
January 2025
Gene Regulation Laboratory, National Institute of Immunology, Aruna Asaf Ali Marg, New Delhi, 110067, India.
Trimethylamine-N-oxide (TMAO) is gut microbiota-derived metabolite, plays a critical role in human health and diseases such as metabolic, cardiovascular, colorectal cancer and, neurological disorders. Binding interactions between TMAO and serum albumins are crucial to understand the impact of TMAO on disease mechanisms. However, detailed insights into the interaction mechanisms, preferred binding locations, and conformational changes in BSA upon binding TMAO are still unclear.
View Article and Find Full Text PDFCurr Res Microb Sci
December 2024
Department of Orthodontics, Nihon University of Dental School at Matsudo. Chiba 271-8587, Japan.
The SARS-CoV-2 infection has spread to various areas of the world, and the number of infected people, seriously ill people, and deaths have increased in 2020∼2023. It is important to suppress the spread of virus from infected people to non-infected people in order to prevent the disease from becoming more severe. To protect widespread of virus, flavor/fragrances composition was selected as a convenient effective material to protect the inhibition.
View Article and Find Full Text PDFActa Biomater
January 2025
Hainan Cancer Center and Tumor Institute, The First Affiliated Hospital of Hainan Medical University, Haikou 570102, China. Electronic address:
In situ vaccine (ISV) can activate the anti-tumor immune system by inducing immunogenic cell death (ICD) at the tumor site. However, the development of tumor ISV still faces challenges due to insufficient tumor antigens released by tumor cells and the existence of tumor immunosuppressive microenvironment (TIME). Targeting the STING pathway has been reported to enhance the adjuvant effects of in situ tumor vaccines by initiating innate immunity.
View Article and Find Full Text PDFACS Omega
January 2025
Department of Chemical Engineering, Istanbul Technical University, Istanbul 34469, Türkiye.
In this study, a bovine serum albumin (BSA)-coated magnetic single-walled carbon nanotube (mCNT) was synthesized using covalent functionalization. Mitoxantrone (MTO) was chosen as a model drug, and loading/release profiles of mCNTs were evaluated. To synthesize BSA-coated mCNT, 1-ethyl-3-(3-(dimethylamino)propyl) carbodiimide and -hydroxysuccinimide were used as cross-linking agents.
View Article and Find Full Text PDFACS Omega
January 2025
Department of Medicine, School of Medicine, Case Western Reserve University, Cardiovascular Research Institute, Cleveland 44106-7078, United States.
We have developed two monoclonal antibodies, CPTC-2MeSC-1 and CPTC-2MeSC-2, against itaconate and its conjugates with sulfhydryl-containing biomolecules such as cysteines. Itaconate is a dicarboxylic acid metabolite that has recently gained much interest for its anti-inflammatory properties in many biological models. We have synthesized an itaconate-cysteine conjugate ITA-Cys designed to mimic in vivo Michael adducts of itaconate.
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