Self-assembled extracellular matrix protein networks by microcontact printing.
Physiological patterns of the extracellular matrix protein, laminin-1, were obtained on glass substrates by physisorption-assisted microcontact printing. Besides the well-retained antigenicity confirmed by indirect immunofluorescence assays, we investigated the supramolecular organization of the proteins by atomic force microscopy. We found the characteristic protein self-assembling in polygonal networks with well-defined sub-100 nm quaternary structures of laminin. The formation of these physiological mesh-like protein matrices was obtained by means of one-step soft lithography without any preliminary functionalization of glass, which can be exploited for many possible applications for cell cultures and biomolecular devices.
Sgarbi
Nicoletta
N
NNL, National Nanotechnology Laboratory of Istituto Nazionale di Fisica della Materia, c/o Dipartimento di Ingegneria dell'Innovazione, Università di Lecce, via Arnesano, Lecce I-73100, Italy. nicoletta.sgarbi@unile.it
Pisignano
Dario
D
Di Benedetto
Francesca
F
Gigli
Giuseppe
G
Cingolani
Roberto
R
Rinaldi
Ross
R
D020099:Coated Materials, Biocompatible / Q000138:chemical synthesis* / Q000737:chemistry; D003460:Crystallization / Q000379:methods*; D016326:Extracellular Matrix Proteins / Q000737:chemistry; D007797:Laminin / Q000737:chemistry* / Q000648:ultrastructure*; D008422:Materials Testing; D011487:Protein Conformation; D023822:Tissue Engineering / Q000379:methods*
D020099:Coated Materials, Biocompatible; D016326:Extracellular Matrix Proteins; D007797:Laminin