Textile Functionalization by Porous Protein Crystal Conjugation and Guest Molecule Loading

Author:

Hartje Luke F.1,Andales David A.2,Gintner Lucas P.2,Johnson Lucas B.2,Li Yan V.3ORCID,Snow Christopher D.12ORCID

Affiliation:

1. Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523, USA

2. Department of Chemical and Biological Engineering, Colorado State University, Fort Collins, CO 80523, USA

3. Department of Design and Merchandizing, Colorado State University, Fort Collins, CO 80523, USA

Abstract

Protein crystals are versatile nanostructured materials that can be readily engineered for applications in nanomedicine and nanobiotechnology. Despite their versatility, the small size of typical individual protein crystals (less than one cubic mm) presents challenges for macroscale applications. One way to overcome this limitation is by immobilizing protein crystals onto larger substrates. Cotton is composed primarily of cellulose, the most common natural fiber in the world, and is routinely used in numerous material applications including textiles, explosives, paper, and bookbinding. Here, two types of protein crystals were conjugated to the cellulosic substrate of cotton fabric using a 1,1′-carbonyldiimidazole/aldehyde mediated coupling protocol. The efficacy of this attachment was assessed via accelerated laundering and quantified by fluorescence imaging. The ability to load guest molecules of varying sizes into the scaffold structure of the conjugated protein crystals was also assessed. This work demonstrates the potential to create multifunctional textiles by incorporating diverse protein crystal scaffolds that can be infused with a multiplicity of useful guest molecules. Cargo molecule loading and release kinetics will depend on the size of the guest molecules as well as the protein crystal solvent channel geometry. Here, we demonstrate the loading of a small molecule dye into the small pores of hen egg white lysozyme crystals and a model enzyme into the 13-nm pores delimited by “CJ” crystals composed of an isoprenoid-binding protein from Campylerbacter jejuni.

Funder

National Science Foundation

Publisher

MDPI AG

Subject

Inorganic Chemistry,Condensed Matter Physics,General Materials Science,General Chemical Engineering

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