[Langmuir] Spatially Addressable Chemoselective C-Terminal Ligation of an Intein Fusion Protein from a Complex Mixture to a Hydrazine-Terminated Surface
writer：Peng Yang, Stella M. Marinakos, and Ashutosh Chilkoti
keywords：doi. 10.1021/la104186n
source：期刊
specific source：Langmuir (Supramolecular Chemistry at Interfaces Special Issue)
Issue time：2010年
Protein immobilization on surfaces is useful in many areas of research, including biological characterization, antibody purification, and clinical diagnostics. A critical limitation in the development of protein microarrays and heterogeneous protein-based assays is the enormous amount of work and associated costs in the purification of proteins prior to their immobilization onto a surface. Methods to address this problem would simplify the development of interfacial diagnostics that use a protein as the recognition element. Herein, we describe an approach to the facile, site- specific immobilization of proteins on a surface without any preprocessing or sample purification steps that ligates an intein fusion protein at its C-terminus by reaction with a hydrazine group presented by a surface. Furthermore, we demonstrate that this methodology can directly immobilize a protein directly from cell lysate onto a protein-resistant surface. This methodology is also compatible with soft lithography and inkjet printing so that one or more proteins can be patterned on a surface without the need for purification.