Silk-based blood stabilization for diagnostics

Proc Natl Acad Sci U S A. 2016 May 24;113(21):5892-7. doi: 10.1073/pnas.1602493113. Epub 2016 May 9.

Abstract

Advanced personalized medical diagnostics depend on the availability of high-quality biological samples. These are typically biofluids, such as blood, saliva, or urine; and their collection and storage is critical to obtain reliable results. Without proper temperature regulation, protein biomarkers in particular can degrade rapidly in blood samples, an effect that ultimately compromises the quality and reliability of laboratory tests. Here, we present the use of silk fibroin as a solid matrix to encapsulate blood analytes, protecting them from thermally induced damage that could be encountered during nonrefrigerated transportation or freeze-thaw cycles. Blood samples are recovered by simple dissolution of the silk matrix in water. This process is demonstrated to be compatible with a number of immunoassays and provides enhanced sample preservation in comparison with traditional air-drying paper approaches. Additional processing can remediate interactions with conformational structures of the silk protein to further enhance blood stabilization and recovery. This approach can provide expanded utility for remote collection of blood and other biospecimens empowering new modalities of temperature-independent remote diagnostics.

Keywords: blood; diagnostics; protein; silk; stabilization.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Biomarkers / blood
  • Blood Proteins / analysis*
  • Dried Blood Spot Testing / methods*
  • Enzyme-Linked Immunosorbent Assay
  • Fibroins / chemistry*
  • Humans
  • Immunoglobulin E / blood*
  • Lipocalin-2 / blood*
  • Molecular Diagnostic Techniques
  • Protein Stability
  • Temperature
  • Water / chemistry

Substances

  • Biomarkers
  • Blood Proteins
  • LCN2 protein, human
  • Lipocalin-2
  • Water
  • Immunoglobulin E
  • Fibroins