caa a22 4500 606215638 CHVBK 20210128101059.0 cr unu---uuuuu 210128e20150401xx s 000 0 eng 10.1007/s00701-015-2368-x doi (NATIONALLICENCE)springer-10.1007/s00701-015-2368-x Higher impact energy in traumatic brain injury interferes with noncovalent and covalent bonds resulting in cytotoxic brain tissue edema as measured with computational simulation [Elektronische Daten] [Hans von Holst, Xiaogai Li] Background: Cytotoxic brain tissue edema is a complicated secondary consequence of ischemic injury following cerebral diseases such as traumatic brain injury and stroke. To some extent the pathophysiological mechanisms are known, but far from completely. In this study, a hypothesis is proposed in which protein unfolding and perturbation of nucleotide structures participate in the development of cytotoxic edema following traumatic brain injury (TBI). Methods: An advanced computational simulation model of the human head was used to simulate TBI. The consequences of kinetic energy transfer following an external dynamic impact were analyzed including the intracranial pressure (ICP), strain level, and their potential influences on the noncovalent and covalent bonds in folded protein structures. Results: The result shows that although most of the transferred kinetic energy is absorbed in the skin and three bone layers, there is a substantial amount of energy reaching the gray and white matter. The kinetic energy from an external dynamic impact has the theoretical potential to interfere not only with noncovalent but also covalent bonds when high enough. The induced mechanical strain and pressure may further interfere with the proteins, which accumulate water molecules into the interior of the hydrophobic structures of unfolded proteins. Simultaneously, the noncovalent energy-rich bonds in nucleotide adenosine-triphosphates may be perturbed as well. Conclusions: Based on the analysis of the numerical simulation data, the kinetic energy from an external dynamic impact has the theoretical potential to interfere not only with noncovalent, but also with covalent bonds when high enough. The subsequent attraction of increased water molecules into the unfolded protein structures and disruption of adenosine-triphosphate bonds could to some extent explain the etiology to cytotoxic edema. Springer-Verlag Wien, 2015 Cytotoxic edema nationallicence Kinetic energy nationallicence Noncovalent and covalent bonds nationallicence Unfolded protein nationallicence Adenosine-triphosphate nationallicence von Holst Hans Section of Neurosurgery, Division of Clinical Neuroscience, Karolinska Institutet, Stockholm, Sweden aut Li Xiaogai Division of Neuronic Engineering, School of Technology and Health, Royal Institute of Technology (KTH), Stockholm, Sweden aut Acta Neurochirurgica Springer Vienna 157/4(2015-04-01), 639-648 0001-6268 157:4<639 2015 157 701 https://doi.org/10.1007/s00701-015-2368-x text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 research-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00701-015-2368-x text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- von Holst Hans Section of Neurosurgery, Division of Clinical Neuroscience, Karolinska Institutet, Stockholm, Sweden aut NATIONALLICENCE 700 1- Li Xiaogai Division of Neuronic Engineering, School of Technology and Health, Royal Institute of Technology (KTH), Stockholm, Sweden aut NATIONALLICENCE 773 0- Acta Neurochirurgica Springer Vienna 157/4(2015-04-01), 639-648 0001-6268 157:4<639 2015 157 701