Primary biomolecular adsorption energetics of core-shell nanocomplexes: Implications for biological interactions

• 成果类型: Article
• 署名作者: Lilova, Kristina; Subramani, Tamilarasan; Montini, Isabella; Harrison, Anne; Scharrer, Manuel; Wu, Jun; Xu, Hongwu; Navrotsky, Alexandra
• 署名单位: Arizona State University; Arizona State University-Tempe; Arizona State University; Arizona State University-Tempe; Oregon State University; Arizona State University; Arizona State University-Tempe; University of Tennessee System; University of Tennessee Knoxville
• 刊物名称: PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
• ISSN/ISSBN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.2535339123
• 发表日期: 2026-03-10
• 页码: e2535339123
• 关键词: core-shell nanocomplex; biomolecular adsorption energetics; surface functionalization; drug delivery nanocarriers; enthalpy of hydration; PROTEIN ADSORPTION; MAGNETITE NANOPARTICLES; SERUM-ALBUMIN; delivery; hydration; DYNAMICS

摘要

Molecular organization at the nano- bio interface governing the colloidal stability, reactivity, immune recognition, and drug delivery performance of nanoparticles remains difficult to predict. Quantifying the primary hydration energetics of biomolecule- coated nanomaterials can determine those interactions and provide a basis for engineered nanocarriers with tailored behavior in biological systems. Here, we measured the thermodynamics of water adsorption on patchy dry magnetite (Fe3O4) nanoparticles coated with three model biomolecules, bovine serum albumin, potato starch, and lauric acid and compared these properties to the hydration energetics of the corresponding free dry biomolecules. The results demonstrate how the surface functionalization alters the hydrophilicity, the accessible hydrophilic surface, and the interaction potential of the nanocomplex surface with biological media. The protein coating increases the interaction potential of the surface of the nanocomplex. The weaker interaction potential of the polysaccharide coating and the relatively large hydrophilic surface area allow dynamic and reversible binding, while the fatty acid rearranges into a partial bilayer with very strong hydrophilicity. The findings establish the hydration enthalpy as a quantitative basis to determine and interpret nanoparticle interactions with proteins, membranes, and biological fluids, and provide a thermodynamic foundation for designing nanocarriers with predictable biological reactivity.