Stabilization of viruses by encapsulation in silk proteins

ACS Appl Mater Interfaces. 2014 Oct 22;6(20):18189-96. doi: 10.1021/am5051873. Epub 2014 Oct 1.

Abstract

Viruses are important for a range of modern day applications. However, their utility is limited by their susceptibility to temperature degradation. In this study, we report a simple system to compare the ability of different dried protein films to stabilize viruses against exposure to elevated temperatures. Films from each of three different silks, silkworm, honeybee silk and hornet silk, stabilized entrapped viruses at 37 °C better than films of albumin from bovine serum (BSA) and all four proteins provided substantially more stabilization than no protein controls. A comparison of the molecular structure of the silks and BSA films showed no correlation between the ability of the proteins to stabilize the virus and the secondary structure of the protein in the films. The mechanism of stabilization is discussed and a hypothesis is suggested to explain the superior performance of the silk proteins.

Keywords: FTIR; bacteriophage; biocontrol; coiled coil; protein stability; vaccine stabilization.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bees
  • Cattle
  • Microbial Viability
  • Protein Conformation
  • Serum Albumin, Bovine / metabolism
  • Silk / chemistry*
  • Spectrophotometry, Infrared
  • Temperature
  • Viruses / chemistry*
  • Viruses / pathogenicity
  • Water / chemistry

Substances

  • Silk
  • Water
  • Serum Albumin, Bovine