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<p>In this research, we focused the detailed study of the interaction and bio-conjugate formation of grown NIR responsive nanostructured Cu<sub>2</sub>ZnSnS<sub>4</sub> (CZTS) and Cu<sub>2</sub>ZnSnSe<sub>4</sub> (CZTSe) with model bovine serum albumin (BSA) protein. The dynamics of binding showed that corona formation time for CZTS NPs-BSA (~ 806&#xa0;min) was larger than CZTSe NPs-BSA (~ 15&#xa0;min). Time for reorganization of BSA due to binding with CZTS NPs (~ 24&#xa0;min) was much less than that of CZTSe NPs (~ 311&#xa0;min). BSA binding was more significant than unfolding at the interface of CZTS whereas for CZTSe NPs-BSA unfolding was more significant than binding. The protein secondary structural denaturation through quenching and denaturation has been observed. In case of CZTSe NPs-BSA, the strong positive cooperative reaction (<i>n</i> ~ 1.95) was more prominent than CZTS NPs-BSA (<i>n</i> ~ 1.44). Both Trp and Tyr residues responded at the surface of CZTS whereas only Trp responded at the surface of CZTSe during quenching of protein. CZTS NPs-BSA showed formation of both soft and hard corona, whereas very small sizes CZTSe NPs (~ 5&#xa0;nm) were selectively formed hard corona on their surface. The average ultrafast life time (τ) of CZTS NPs-BSA varied from 3.76 ns to 3 ns, whereas CZTSe NPs-BSA showed life time (τ) variation from 3.75 ns to 3.53 ns.</p>

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Interaction and Binding of Protein with Cu2ZnSnS4 and Cu2ZnSnSe4 Chalcogenide NIR Semiconducting Nanoparticles

  • 期刊论文

  • 发表日期：

    2025年12月1日

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  • Rudra Narayan Mondal,
  • Rajesh Samui,
  • Satyajit Saha,
  • Amit Kumar Bhunia

摘要

In this research, we focused the detailed study of the interaction and bio-conjugate formation of grown NIR responsive nanostructured Cu2ZnSnS4 (CZTS) and Cu2ZnSnSe4 (CZTSe) with model bovine serum albumin (BSA) protein. The dynamics of binding showed that corona formation time for CZTS NPs-BSA (~ 806 min) was larger than CZTSe NPs-BSA (~ 15 min). Time for reorganization of BSA due to binding with CZTS NPs (~ 24 min) was much less than that of CZTSe NPs (~ 311 min). BSA binding was more significant than unfolding at the interface of CZTS whereas for CZTSe NPs-BSA unfolding was more significant than binding. The protein secondary structural denaturation through quenching and denaturation has been observed. In case of CZTSe NPs-BSA, the strong positive cooperative reaction (n ~ 1.95) was more prominent than CZTS NPs-BSA (n ~ 1.44). Both Trp and Tyr residues responded at the surface of CZTS whereas only Trp responded at the surface of CZTSe during quenching of protein. CZTS NPs-BSA showed formation of both soft and hard corona, whereas very small sizes CZTSe NPs (~ 5 nm) were selectively formed hard corona on their surface. The average ultrafast life time (τ) of CZTS NPs-BSA varied from 3.76 ns to 3 ns, whereas CZTSe NPs-BSA showed life time (τ) variation from 3.75 ns to 3.53 ns.