Textile Functionalization by Porous Protein Crystal Conjugation and Guest Molecule Loading

被引:4
作者
Hartje, Luke F. [1 ]
Andales, David A. [2 ]
Gintner, Lucas P. [2 ]
Johnson, Lucas B. [2 ]
Li, Yan V. [3 ]
Snow, Christopher D. [1 ,2 ]
机构
[1] Colorado State Univ, Dept Biochem & Mol Biol, Ft Collins, CO 80523 USA
[2] Colorado State Univ, Dept Chem & Biol Engn, Ft Collins, CO 80523 USA
[3] Colorado State Univ, Dept Design & Merchandizing, Ft Collins, CO 80523 USA
基金
美国国家科学基金会;
关键词
protein crystals; crosslinking; host-guest crystals; bioconjugation; textile engineering; LINKED ENZYME CRYSTALS; SEPARATION; DIFFUSION; LYSOZYME; SUBTILISIN; CATALYSTS; DELIVERY; PLATFORM; RELEASE; CLEC;
D O I
10.3390/cryst13020352
中图分类号
O7 [晶体学];
学科分类号
0702 ; 070205 ; 0703 ; 080501 ;
摘要
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.
引用
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页数:12
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