Mechanism of Stabilization of Labile Compounds by Silk Fibroin Proteins
Technical Report,01 Nov 2013,31 Oct 2016
Trustees Of Tufts College Inc Somerville
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The objective of this research was to elucidate the fundamental mechanisms by which labile compounds are entrapped and stabilized by silk fibroin protein. The plans built upon our previous studies with silk fibroin for enzyme and antibody stabilization and define the critical interactions between the silk protein matrix and introduced compounds that promote long term stability. An understanding of how the unique chemical and structural features of the silk fibroin stabilize compounds allow for a comparison with more traditional stabilizing agents and shed light on the incompletely understood conditions that lead to stability of labile molecules. During this project, we utilized proteins in blood as a test system to study and understand the role of silk in the stabilization of a range of different analytes, including entrapment, storage and recovery. Here, we successfully used silk fibroin as a solid matrix to encapsulate blood analytes, protecting them from thermally induced damage that can be encountered during transportation or freeze-thaw cycle.