Bacterial protein patterning by micro-contact printing of PLL-g-PEG.
Biomimetic micro-patterned surfaces of three S-layer (fusion) proteins, wild type (SbpA), enhanced green fluorescence protein (SbpA-EGFP) and streptavidin (SbpA-STV), were built by microcontact printing of poly-L-lysine grafted polyethylene glycol (PLL-g-PEG). The functionality of the adsorbed proteins was studied with atomic force microscopy and fluorescence microscopy. Atomic force microscopy (AFM) measurements showed that wild-type SbpA recrystallized on PLL-g-PEG free areas, while fluorescent properties of SbpA-EGFP and the interaction of SbpA-streptavidin heterotetramers with biotin were not affected due to the adsorption on the micro patterned substrates.
Saravia
V
V
Chemical Engineering Department, URV, Av. Països Catalans 26, 43007 Tarragona, Spain.
Küpcü
S
S
Nolte
M
M
Huber
C
C
Pum
D
D
Fery
A
A
Sleytr
U B
UB
Toca-Herrera
J L
JL
D001426:Bacterial Proteins / Q000378:metabolism* / Q000648:ultrastructure; D001709:Biotechnology / Q000379:methods*; D001710:Biotin / Q000378:metabolism; D018625:Microscopy, Atomic Force; D008856:Microscopy, Fluorescence; D009004:Monosaccharide Transport Proteins / Q000378:metabolism* / Q000648:ultrastructure; D011092:Polyethylene Glycols / Q000378:metabolism*; D011107:Polylysine / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D019809:Streptavidin / Q000378:metabolism
D001426:Bacterial Proteins; D009004:Monosaccharide Transport Proteins; D011993:Recombinant Fusion Proteins; C120455:SbpA protein, bacteria; D011107:Polylysine; D011092:Polyethylene Glycols; D001710:Biotin; D019809:Streptavidin