Ruggedized peptide receptors for soldier health and performance monitoring

Matthew B. Coppock; Dimitra N. Stratis-Cullum

doi:10.1117/12.2518631

2 May 2019 Ruggedized peptide receptors for soldier health and performance monitoring

Matthew B. Coppock, Dimitra N. Stratis-Cullum

Proceedings Volume 11020, Smart Biomedical and Physiological Sensor Technology XVI; 110200M (2019) https://doi.org/10.1117/12.2518631
Event: SPIE Defense + Commercial Sensing, 2019, Baltimore, MD, United States

Abstract

As the Army moves towards equipping the soldier with more advanced wearable sensing devices for real-time environmental, health, and performance monitoring, there is a significant need for the biological receptors integrated into such devices capable of consistent performance in multifaceted operational environments. The instability, long development times, and inconsistencies in production of monoclonal antibodies, the gold standard receptors for biological detection, has resulted in the advent of alternative antibody technologies to fill these technological gaps. Protein Catalyzed Capture (PCC) agent technology is capable of the bottom-up development of highly stable and tailorable receptors through iterative in situ ‘click’ chemistry cycles with one-bead-one-compound (OBOC) peptide libraries. Aside from the inherent thermal stability and binding performance comparable to, and oftentimes exceeding, monoclonal antibodies, the modularity of PCCs allows for easy integration into various detection platforms and assays. Capable of full receptor development in ~2 weeks, as highlighted in this proceeding, PCCs can fulfill the need for alternative antibodies by addressing critical gaps in adaptability, manufacturability, and stability.

Conference Presentation

Citation Download Citation

Matthew B. Coppock and Dimitra N. Stratis-Cullum "Ruggedized peptide receptors for soldier health and performance monitoring", Proc. SPIE 11020, Smart Biomedical and Physiological Sensor Technology XVI, 110200M (2 May 2019); https://doi.org/10.1117/12.2518631

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