The potential relationship between chronic traumatic encephalopathy (CTE) and head injuries such as blast-related traumatic brain injury (TBI) is an important area of study, particularly for military and contact sports populations, yet little is known about this relationship. To address this topic, the Department of Defense (DoD) Blast Injury Research Program Coordinating Office organized the 2015 International State-of-the-Science Meeting, which brought together subject matter experts from the DoD, other federal agencies, academia, industry, foreign allies, and the sports community. Over the course of the meeting, this community of experts reached a consensus regarding the current body of knowledge and the future of the field. The overarching finding was that there is insufficient existing scientific evidence to link blast-related

Public reporting burden for the collection of information is estimated to average 1 hour per response, including the time for reviewing instructions, searching existing data sources, gathering and maintaining the data needed, and completing and reviewing the collection of information. Send comments regarding this burden estimate or any other aspect of this collection of information, including suggestions for reducing this burden, to Washington Headquarters Services, Directorate for Information Operations and Reports, 1215 Jefferson Davis Highway, Suite 1204, Arlington VA 22202-4302. Respondents should be aware that notwithstanding any other provision of law, no person shall be subject to a penalty for failing to comply with a collection of information if it does not display a currently valid OMB control number.

A bioanalytical method for evaluating the extent of protein cross-linking was developed. The method is based on reversed-phase HPLC determination of tryptophan released from the cross-linked proteins by Pronase, a nonspecific proteolytic enzyme. The amounts of tryptophan released from un-crosslinked bovine serum albumin (BSA), a nanopeptide, and Trp-Phe in control experiments were consistent with the tryptophan content of the protein and peptides. However, the amount of tryptophan released decreased significantly when BSA was cross-linked extensively by heating at 120 °C in the presence of glucose. The decrease in tryptophan showed a good correlation with the amount of cross-linked BSA that remained insoluble after Pronase digestion, suggesting that tryptophan released by Pronase is a useful measure of the cross-linking and biodegradability of a protein-based biomaterial.