Conformation of microcontact-printed proteins by atomic force microscopy molecular sizing.
We investigated the structural changes occurring in proteins patterned via microcontact printing. This was done by molecular sizing using atomic force microscopy to observe the structure of printed individual metalloprotein molecules in the unlabeled and untreated states. We observed that the size of the printed proteins were more than 2-fold smaller than the native shape, which indicates that some deformations take place upon the contact-assisted adsorption on silanized silicon dioxide. This can be attributed to simultaneously occurring effects, and particularly to the sandwiching between surfaces of very different hydrophilic/hydrophobic properties during contact lithography.
Biasco
Adriana
A
National Nanotechnology Laboratory of Istituto Nazionale di Fisica della Materia, c/o Dipartimento di Ingegneria dell'Innovazione, Università di Lecce, via Arnesano, I-73100 Lecce, Italy. adriana.biasco@unile.it
Pisignano
Dario
D
Krebs
Blandine
B
Pompa
Pier Paolo
PP
Persano
Luana
L
Cingolani
Roberto
R
Rinaldi
Ross
R
D000327:Adsorption; D001400:Azurin / Q000737:chemistry*; D018625:Microscopy, Atomic Force / Q000379:methods*; D010316:Particle Size; D011487:Protein Conformation; D011550:Pseudomonas aeruginosa / Q000737:chemistry; D012680:Sensitivity and Specificity; D012822:Silicon Dioxide / Q000737:chemistry; D013499:Surface Properties
D001400:Azurin; D012822:Silicon Dioxide