Selective recruitment of membrane protein complexes onto gold substrates patterned by dip-pen nanolithography.
Dip-pen nanolithography (DPN) is employed to develop a generic array platform for the selective recruitment of membrane protein complexes. An atomic force microscope tip inked with HS(CH2)16NH2 is used to generate amino-terminated domains on gold. These domains can be arranged into microscopic and submicroscopic patterns, and the untreated gold substrate is subsequently blocked with HS(CH2)2CONH(CH2CH2O)15CH3, a compound known to resist the unspecific binding of proteins and cells. The patterned gold substrate is exposed to an enriched membrane fraction from mutant Rhodobacter sphaeroides, which contains photosynthetic core complexes consisting of the reaction center and the light-harvesting complex LH1. The selective recruitment to the patterned domains, governed primarily by electrostatic interactions, is confirmed by contact mode atomic force microscopy.
Valiokas
Ramūnas
R
Division of Molecular Physics, Department of Physics, Chemistry and Biology, Linköping University, S-581 83 Linköping, Sweden. valiokas@ar.fi.lt
Vaitekonis
Sarūnas
S
Klenkar
Goran
G
Trinkūnas
Gediminas
G
Liedberg
Bo
B
D000327:Adsorption; D001426:Bacterial Proteins / Q000737:chemistry; D006046:Gold / Q000737:chemistry; D008565:Membrane Proteins / Q000737:chemistry*; D018625:Microscopy, Atomic Force; D036103:Nanotechnology / Q000379:methods*; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry*; D012242:Rhodobacter sphaeroides / Q000378:metabolism; D055672:Static Electricity; D013379:Substrate Specificity; D013438:Sulfhydryl Compounds / Q000737:chemistry; D013499:Surface Properties
D001426:Bacterial Proteins; D008565:Membrane Proteins; D011506:Proteins; D013438:Sulfhydryl Compounds; D006046:Gold