期刊
ACS BIOMATERIALS SCIENCE & ENGINEERING
卷 2, 期 11, 页码 1856-1861出版社
AMER CHEMICAL SOC
DOI: 10.1021/acsbiomaterials.6b00447
关键词
microcapsules; protein design; self-assembly; hydrophobin; modular; surface display
资金
- NSF through the Yale Materials Research Science and Engineering Center [MRSEC DMR-1119826]
- Raymond and Beverly Sackler Institute for Biological, Physical and Engineering Sciences
- NSF [CBET-1066904, CHE-1213362, DMR-1307712]
- National Science Foundation Graduate Research Fellowship
- Department of Energy's Office of Biological and Environmental Research (BER)
- National Institute of Health (NIH) [1R01GM10621-01A1]
Proteins are desirable building blocks to create self-assembled, spatially defined structures and interfaces on length-scales that are inaccessible by traditional methods. Here, we describe a novel approach to create functionalized monolayers using the proteins BsIA and SpyCatcher/SpyTag. BsIA is a bacterial hydrophobin whose amphiphilic character underlies its ability to assemble into a monolayer at both air/water and oil/water interfaces. We demonstrate that Bsa1A having the SpyTag peptide fused at the N- or C-terminus does not affect the formation of such monolayers. We establish the creation of stable oil-in-water microcapsules using Bs1A, and also show the fabrication of capsules outwardly displaying the reactive SpyTag peptide by fusing it to the C-terminus of Bs1A. Such capsules can be covalently labeled by reacting the surface-displayed SpyTag with SpyCatcher fused to any desired protein. We demonstrate this principle by labeling microcapsules using green fluorescent protein (GFP). All components are genetically encodable, the reagents can be readily prepared in large quantities, and all reactions occur at ambient temperature in aqueous solution. Thus, this straightforward, modular, scalable strategy has myriad potential applications in the creation of novel, functional materials, and interfaces.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据