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<p>Protein adsorption onto surfaces is a critical process in biomaterial science, influencing subsequent biological responses. Understanding this phenomenon is key to designing materials with controlled interactions for biomedical applications. Here, we report controllable protein adsorption onto crystalline lamellar assemblies of carboxylated cello-oligosaccharides synthesized via cellodextrin phosphorylase-catalyzed oligomerization. These assemblies, featuring a terminal carboxy group linked by alkyl chains, possessed a negative surface charge, the magnitude of which depended on alkyl linker length, pH, and ionic strength, as confirmed by zeta potential measurements. Under varying pH and ionic strength conditions, we observed significant adsorption of basic proteins, which increased with longer alkyl linkers and lower ionic strength. Although acidic protein adsorption at acidic pH was minimal under high ionic strength, we notably found that acidic proteins were adsorbed onto negatively charged assemblies under low ionic strength. Our results demonstrate that electrostatic interactions primarily govern protein adsorption on these assemblies, enabling controllable protein adsorption through the adjustment of their surface properties and solution conditions.</p>

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Electrostatic control of protein adsorption onto negatively charged crystalline cello-oligosaccharide assemblies

  • 期刊论文

  • 发表日期：

    2025年9月22日

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  • Kai Sugiura,
  • Akari Matsunami,
  • Yuuki Hata,
  • Hiroshi Tanaka,
  • Takeshi Serizawa

摘要

Protein adsorption onto surfaces is a critical process in biomaterial science, influencing subsequent biological responses. Understanding this phenomenon is key to designing materials with controlled interactions for biomedical applications. Here, we report controllable protein adsorption onto crystalline lamellar assemblies of carboxylated cello-oligosaccharides synthesized via cellodextrin phosphorylase-catalyzed oligomerization. These assemblies, featuring a terminal carboxy group linked by alkyl chains, possessed a negative surface charge, the magnitude of which depended on alkyl linker length, pH, and ionic strength, as confirmed by zeta potential measurements. Under varying pH and ionic strength conditions, we observed significant adsorption of basic proteins, which increased with longer alkyl linkers and lower ionic strength. Although acidic protein adsorption at acidic pH was minimal under high ionic strength, we notably found that acidic proteins were adsorbed onto negatively charged assemblies under low ionic strength. Our results demonstrate that electrostatic interactions primarily govern protein adsorption on these assemblies, enabling controllable protein adsorption through the adjustment of their surface properties and solution conditions.