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<p>Understanding protein motion within the cell is crucial for predicting reaction rates and macromolecular transport in the cytoplasm. A key question is how crowded environments affect protein dynamics through hydrodynamic and direct interactions at molecular length scales. Using megahertz X-ray Photon Correlation Spectroscopy (MHz-XPCS) at the European X-ray Free Electron Laser (EuXFEL), we investigate ferritin diffusion at microsecond time scales. Our results reveal anomalous diffusion, indicated by the non-exponential decay of the intensity autocorrelation function <i>g</i><sub>2</sub>(<i>q</i>,&#xa0;<i>t</i>) at high concentrations. This behavior is consistent with the presence of cage-trapping between the short- and long-time protein diffusion regimes. Modeling with the <i>δ</i><i>γ</i>-theory of hydrodynamically interacting colloidal spheres successfully reproduces the experimental data by including a scaling factor linked to the protein direct interactions. These findings offer insights into the complex molecular motion in crowded protein solutions, with potential applications for optimizing ferritin-based drug delivery, where protein diffusion is the rate-limiting step.</p>

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Coherent X-rays reveal anomalous molecular diffusion and cage effects in crowded protein solutions

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年11月29日

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  • Anita Girelli,
  • Maddalena Bin,
  • Mariia Filianina,
  • Michelle Dargasz,
  • Nimmi Das Anthuparambil,
  • Johannes Möller,
  • Alexey Zozulya,
  • Iason Andronis,
  • Sonja Timmermann,
  • Sharon Berkowicz,
  • Sebastian Retzbach,
  • Mario Reiser,
  • Agha Mohammad Raza,
  • Marvin Kowalski,
  • Mohammad Sayed Akhundzadeh,
  • Jenny Schrage,
  • Chang Hee Woo,
  • Maximilian D. Senft,
  • Lara Franziska Reichart,
  • Aliaksandr Leonau,
  • Prabhu Rajaiah Prince,
  • William Chèvremont,
  • Tilo Seydel,
  • Jörg Hallmann,
  • Angel Rodriguez-Fernandez,
  • Jan-Etienne Pudell,
  • Felix Brausse,
  • Ulrike Boesenberg,
  • James Wrigley,
  • Mohamed Youssef,
  • Wei Lu,
  • Wonhyuk Jo,
  • Roman Shayduk,
  • Trey Guest,
  • Anders Madsen,
  • Felix Lehmkühler,
  • Michael Paulus,
  • Fajun Zhang,
  • Frank Schreiber,
  • Christian Gutt,
  • Fivos Perakis

摘要

Understanding protein motion within the cell is crucial for predicting reaction rates and macromolecular transport in the cytoplasm. A key question is how crowded environments affect protein dynamics through hydrodynamic and direct interactions at molecular length scales. Using megahertz X-ray Photon Correlation Spectroscopy (MHz-XPCS) at the European X-ray Free Electron Laser (EuXFEL), we investigate ferritin diffusion at microsecond time scales. Our results reveal anomalous diffusion, indicated by the non-exponential decay of the intensity autocorrelation function g2(q, t) at high concentrations. This behavior is consistent with the presence of cage-trapping between the short- and long-time protein diffusion regimes. Modeling with the δγ-theory of hydrodynamically interacting colloidal spheres successfully reproduces the experimental data by including a scaling factor linked to the protein direct interactions. These findings offer insights into the complex molecular motion in crowded protein solutions, with potential applications for optimizing ferritin-based drug delivery, where protein diffusion is the rate-limiting step.