Koundal Sakshi, Pathania Apoorva, Kour Harman Deep, Pathania Anu Radha, Kaur Jatinder, Juneja Bhanu, Sharma Girish Chandra, Bhowmik Abhijit, Santhosh A Johnson
Department of Chemistry (UIS), Chandigarh University, Mohali, Punjab, 140413, India.
Division of Research and Innovation, Department of Electronics and Communication Engineering, Chandigarh Engineering College, Chandigarh Group of Colleges Jhanjeri, Mohali, Punjab, 140307, India.
Sci Rep. 2025 Apr 8;15(1):11997. doi: 10.1038/s41598-025-93108-z.
Activates the pituitary gland, leading to increased secretion of growth hormone. This activation plays a crucial role in growth, metabolism, and tissue repair. Bovine serum albumin, a well-studied protein, demonstrates the interaction between proteins-ligands and transports various compounds in the bloodstream. This study elucidates the molecular interactions between L-ornithine and BSA through spectroscopic analysis, identifying binding modes, constants, and structural changes. Molecular docking techniques are employed to correlate with experimental data from fluorescence and UV spectroscopy analyses.The study uses Fourier transform infrared spectroscopy, UV-Visible spectroscopy, fluorescence spectroscopy, circular dichroism spectroscopy and molecular docking to analyze the interaction between bovine serum albumin and L-ornithine, providing thermodynamic parameters for understanding the protein structure and its binding.The interactions between L-ornithine and bovine serum albumin (BSA) were characterized using UV-visible spectroscopy, which demonstrated a hyperchromic shift. Fluorescence spectroscopy revealed that L-ornithine quenches the intrinsic fluorescence of both BSA and human serum albumin (HSA) via a static quenching mechanism, resulting in the formation of stable BSA-L-ornithine and HSA-L-ornithine complexes. Furthermore, Fourier-transform infrared (FTIR) and circular dichroism (CD) spectroscopy indicated a decrease in the secondary structure of the proteins, as evidenced by shifts in the amide II band and a concomitant reduction in α-helix content. Molecular docking studies suggested that L-ornithine binds to BSA within subdomain II. Collectively, these findings provide valuable insights into the metabolic pathways of L-ornithine and its potential pharmacological relevance. The study involves more precise information which revealing the insight of L-ornithine bioavailability. The finding enhances our understanding of interaction with potential implications for drug delivery.
激活垂体，导致生长激素分泌增加。这种激活在生长、新陈代谢和组织修复中起着关键作用。牛血清白蛋白是一种经过充分研究的蛋白质，它展示了蛋白质 - 配体之间的相互作用，并在血液中运输各种化合物。本研究通过光谱分析阐明了L - 鸟氨酸与牛血清白蛋白之间的分子相互作用，确定了结合模式、常数和结构变化。采用分子对接技术与荧光和紫外光谱分析的实验数据相关联。该研究使用傅里叶变换红外光谱、紫外可见光谱、荧光光谱、圆二色光谱和分子对接来分析牛血清白蛋白与L - 鸟氨酸之间的相互作用，为理解蛋白质结构及其结合提供热力学参数。利用紫外可见光谱对L - 鸟氨酸与牛血清白蛋白（BSA）之间的相互作用进行了表征，结果显示有增色效应。荧光光谱表明，L - 鸟氨酸通过静态猝灭机制猝灭了BSA和人血清白蛋白（HSA）的内在荧光，导致形成稳定的BSA - L - 鸟氨酸和HSA - L - 鸟氨酸复合物。此外，傅里叶变换红外（FTIR）光谱和圆二色（CD）光谱表明蛋白质二级结构减少，酰胺II带的位移以及α - 螺旋含量的相应减少证明了这一点。分子对接研究表明L - 鸟氨酸在亚结构域II内与BSA结合。总的来说，这些发现为L - 鸟氨酸的代谢途径及其潜在的药理学相关性提供了有价值的见解。该研究涉及更精确的信息，揭示了L - 鸟氨酸生物利用度的见解。这一发现增强了我们对其相互作用的理解，对药物递送具有潜在意义。
