PDF(Pubmed)
Abstract：
Dendrimers, intricate macromolecules with highly branched nanostructures, offer unique attributes including precise control over size, shape, and functionality, making them promising candidates for a wide range of biomedical applications. The exploration of their interaction with biological environments, particularly human serum albumin (HSA), holds significant importance for biomedical utilization. In this study, the interaction between HSA and a recently developed self-assembling amphiphilic dendrimer (AD) was investigated using various experimental techniques. Fluorescence spectroscopy and isothermal titration calorimetry revealed moderate interactions between the protein and the AD nanomicelles (NMs), primarily attributed to favorable enthalpic contributions arising from electrostatic interactions and hydrogen bonding. Structural analysis indicated minimal changes in HSA upon complexation with the AD NMs, which was further supported by computational simulations demonstrating stable interactions at the atomistic level. These findings provide valuable insights into the binding mechanisms and thermodynamic parameters governing HSA/AD NM interactions, thereby contributing to the understanding of their potential biomedical applications.
摘要：
树枝状聚合物,具有高度支化纳米结构的复杂大分子，提供独特的属性，包括对尺寸的精确控制，形状,和功能，使它们成为广泛的生物医学应用的有前途的候选人。探索它们与生物环境的相互作用，特别是人血清白蛋白（HSA），对生物医学利用具有重要意义。在这项研究中,使用各种实验技术研究了HSA与最近开发的自组装两亲性树枝状聚合物（AD）之间的相互作用。荧光光谱和等温滴定量热法揭示了蛋白质与AD纳米胶束（NMs）之间的中等相互作用，主要归因于静电相互作用和氢键产生的有利焓贡献。结构分析表明HSA与ADNMs复合后变化最小，这得到了计算模拟的进一步支持，证明了在原子水平上的稳定相互作用。这些发现为控制HSA/ADNM相互作用的结合机制和热力学参数提供了有价值的见解，从而有助于理解其潜在的生物医学应用。
