Using liquid crystals to report membrane proteins captured by affinity microcontact printing from cell lysates and membrane extracts.
The chemical heterogeneity of proteins makes development of general and facile surface-based methods for protein analysis a substantial challenge, particularly when analyzing transmembrane proteins. Here, we report a simple surface-based procedure that permits detection of transmembrane proteins from crude cell lysates and cell membrane extracts. The method relies on the use of thermotropic liquid crystals to amplify and report the presence of the transmembrane proteins captured by an affinity ligand on the surface of an elastomeric stamp. A merit of this approach is that the proteins can be imaged on surfaces without requiring the use of matched pairs of antibodies, labels, or complex instrumentation. Detection of epidermal growth factor receptor, a transmembrane glycoprotein, is demonstrated.
Jang
Chang-Hyun
CH
Department of Chemical and Biological Engineering,University of Wisconsin-Madison, Madison, Wisconsin 53706, USA.
Tingey
Matthew L
ML
Korpi
Nichole L
NL
Wiepz
Gregory J
GJ
Schiller
Joan H
JH
Bertics
Paul J
PJ
Abbott
Nicholas L
NL
D000345:Affinity Labels / Q000737:chemistry*; D002457:Cell Extracts / Q000737:chemistry*; D002462:Cell Membrane / Q000737:chemistry*; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003460:Crystallization; D066246:ErbB Receptors / Q000737:chemistry*; D008565:Membrane Proteins / Q000737:chemistry*; D008567:Membranes, Artificial; D013499:Surface Properties
D000345:Affinity Labels; D002457:Cell Extracts; D008565:Membrane Proteins; D008567:Membranes, Artificial; D066246:ErbB Receptors