Textile Functionalization by Porous Protein Crystal Conjugation and Guest Molecule Loading

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.

Porous protein crystals: synthesis and applications

“…In pursuit of multifunctional textiles involving attachment of protein crystal depots, Hartje et al from our group recently demonstrated integration of individual lysozyme and CJ crystals on bulk cotton, via chemical cross-linking with dihydrazides or dialdehydes, respectively. 194 The resulting crystals were able to adsorb guest sulforhodamine-labeled cytochrome P450 protein, although the activity of guest P450 enzyme was not tested. Despite repeated laundering of the functionalized fabrics, at least 20% of the attached crystals were retained when chemically cross-linked to fabric.…”

“…Despite repeated laundering of the functionalized fabrics, at least 20% of the attached crystals were retained when chemically cross-linked to fabric. 194 The authors suggest that journal is © The Royal Society of Chemistry 2024 crystal retention might be improved via more robust chemical crosslinking; 194 additional strategies could involve in situ crystal growth on the surface of the fabric, which could reduce downstream handling and transfer of crystals. This approach may enable additional functionalization of cloth surfaces, particularly when combined with biosensing crystals or scaffolds which interact with specific pathogens.…”