Protein Diffusion and Stokes-Einstein Deviation in Supercooled Cryoprotectant Solutions

Fuente: arXiv
Gespeichert in:
Bibliographische Detailangaben
Hauptverfasser: Bin, Maddalena, Girelli, Anita, Filianina, Mariia, Reiser, Mario, Berkowicz, Sharon, Åhlfeldt, Milla, Dargasz, Michelle, Timmermann, Sonja, Savelkouls, Jaqueline, Kawasaki, Takeshi, Saito, Shinji, Zontone, Federico, Chushkin, Yuriy, Zhang, Fajun, Schreiber, Frank, Paulus, Michael, Gutt, Christian, Perakis, Fivos
Format: Preprint
Veröffentlicht: 2025
Schlagworte:
Online-Zugang:
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
_version_ 1866912743281393664
author Bin, Maddalena
Girelli, Anita
Filianina, Mariia
Reiser, Mario
Berkowicz, Sharon
Åhlfeldt, Milla
Dargasz, Michelle
Timmermann, Sonja
Savelkouls, Jaqueline
Kawasaki, Takeshi
Saito, Shinji
Zontone, Federico
Chushkin, Yuriy
Zhang, Fajun
Schreiber, Frank
Paulus, Michael
Gutt, Christian
Perakis, Fivos
author_facet Bin, Maddalena
Girelli, Anita
Filianina, Mariia
Reiser, Mario
Berkowicz, Sharon
Åhlfeldt, Milla
Dargasz, Michelle
Timmermann, Sonja
Savelkouls, Jaqueline
Kawasaki, Takeshi
Saito, Shinji
Zontone, Federico
Chushkin, Yuriy
Zhang, Fajun
Schreiber, Frank
Paulus, Michael
Gutt, Christian
Perakis, Fivos
contents Vitrification during cryopreservation requires a detailed understanding of the dynamic behavior of biological solutions. We investigate ferritin diffusion in glycerol-water mixtures at supercooled temperatures using X-ray Photon Correlation Spectroscopy (XPCS). Diffusion coefficients were measured from ambient conditions to $T = 210$ K and analyzed using the Vogel-Fulcher-Tammann (VFT) relation, yielding an arrest temperature of $T_0 = 85 \pm 11$ K for ferritin ($R_{\rm h} = 7.3$ nm), markedly lower than $T_0 = 122 \pm 4$ K for larger nanoparticles ($R_{\rm h} = 50$ nm). Below $T \approx 230$ K, ferritin diffusion exceeds the Stokes-Einstein prediction by up to a factor of 2.7, revealing nanoscale deviations from bulk viscosity. A fluctuating-friction model quantitatively links this enhancement to local friction heterogeneity, with fluctuations increasing upon cooling and reaching $\sim 80\%$ of the mean friction at $T=210$ K. These results establish a molecular-scale connection between protein diffusion and solvent dynamical heterogeneity in cryoprotected solutions.
format Preprint
id arxiv_https___arxiv_org_abs_2512_02742
institution arXiv
publishDate 2025
record_format arxiv
spellingShingle Protein Diffusion and Stokes-Einstein Deviation in Supercooled Cryoprotectant Solutions
Bin, Maddalena
Girelli, Anita
Filianina, Mariia
Reiser, Mario
Berkowicz, Sharon
Åhlfeldt, Milla
Dargasz, Michelle
Timmermann, Sonja
Savelkouls, Jaqueline
Kawasaki, Takeshi
Saito, Shinji
Zontone, Federico
Chushkin, Yuriy
Zhang, Fajun
Schreiber, Frank
Paulus, Michael
Gutt, Christian
Perakis, Fivos
Soft Condensed Matter
Vitrification during cryopreservation requires a detailed understanding of the dynamic behavior of biological solutions. We investigate ferritin diffusion in glycerol-water mixtures at supercooled temperatures using X-ray Photon Correlation Spectroscopy (XPCS). Diffusion coefficients were measured from ambient conditions to $T = 210$ K and analyzed using the Vogel-Fulcher-Tammann (VFT) relation, yielding an arrest temperature of $T_0 = 85 \pm 11$ K for ferritin ($R_{\rm h} = 7.3$ nm), markedly lower than $T_0 = 122 \pm 4$ K for larger nanoparticles ($R_{\rm h} = 50$ nm). Below $T \approx 230$ K, ferritin diffusion exceeds the Stokes-Einstein prediction by up to a factor of 2.7, revealing nanoscale deviations from bulk viscosity. A fluctuating-friction model quantitatively links this enhancement to local friction heterogeneity, with fluctuations increasing upon cooling and reaching $\sim 80\%$ of the mean friction at $T=210$ K. These results establish a molecular-scale connection between protein diffusion and solvent dynamical heterogeneity in cryoprotected solutions.
title Protein Diffusion and Stokes-Einstein Deviation in Supercooled Cryoprotectant Solutions
topic Soft Condensed Matter
url https://arxiv.org/abs/2512.02742