Accession Number : AD1031627


Title :   Mechanism of Stabilization of Labile Compounds by Silk Fibroin Proteins


Descriptive Note : Technical Report,01 Nov 2013,31 Oct 2016


Corporate Author : Trustees Of Tufts College Inc Somerville


Personal Author(s) : Kaplan,David


Full Text : https://apps.dtic.mil/dtic/tr/fulltext/u2/1031627.pdf


Report Date : 05 Apr 2017


Pagination or Media Count : 8


Abstract : 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.


Descriptors :   proteins , SILK , blood , scientific research , Stabilization


Subject Categories : Biochemistry


Distribution Statement : APPROVED FOR PUBLIC RELEASE