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Numerical Impact Simulation of Gradually Increased Kinetic Energy Transfer Has the Potential To Break Up Folded Protein Structures Resulting in Cytotoxic Brain Tissue Edema
KTH, School of Technology and Health (STH), Neuronic Engineering.
KTH, School of Technology and Health (STH), Neuronic Engineering.
2013 (English)In: Journal of Neurotrauma, ISSN 0897-7151, E-ISSN 1557-9042, Vol. 30, no 13, 1192-1199 p.Article in journal (Refereed) Published
Abstract [en]

Although the consequences of traumatic brain injury (TBI) and its treatment have been improved, there is still a substantial lack of understanding the mechanisms. Numerical simulation of the impact can throw further lights on site and mechanism of action. A finite element model of the human head and brain tissue was used to simulate TBI. The consequences of gradually increased kinetic energy transfer was analyzed by evaluating the impact intracranial pressure (ICP), strain level, and their potential influences on binding forces in folded protein structures. The gradually increased kinetic energy was found to have the potential to break apart bonds of Van der Waals in all impacts and hydrogen bonds at simulated impacts from 6 m/s and higher, thereby superseding the energy in folded protein structures. Further, impacts below 6 m/s showed none or very slight increase in impact ICP and strain levels, whereas impacts of 6 m/s or higher showed a gradual increase of the impact ICP and strain levels reaching over 1000 KPa and over 30%, respectively. The present simulation study shows that the free kinetic energy transfer, impact ICP, and strain levels all have the potential to initiate cytotoxic brain tissue edema by unfolding protein structures. The definition of mild, moderate, and severe TBI should thus be looked upon as the same condition and separated only by a gradual severity of impact.

Place, publisher, year, edition, pages
2013. Vol. 30, no 13, 1192-1199 p.
Keyword [en]
cytotoxic brain edema, traumatic brain injury, finite element modeling, kinetic energy, protein folding/unfolding
National Category
Medical and Health Sciences
URN: urn:nbn:se:kth:diva-125864DOI: 10.1089/neu.2012.2730ISI: 000321186400010ScopusID: 2-s2.0-84878779356OAI: diva2:641268

QC 20130816

Available from: 2013-08-16 Created: 2013-08-15 Last updated: 2013-08-16Bibliographically approved

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