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Self-assembled extracellular matrix protein networks by microcontact printing

TitoloSelf-assembled extracellular matrix protein networks by microcontact printing
Tipo di pubblicazioneArticolo su Rivista peer-reviewed
Anno di Pubblicazione2004
AutoriSgarbi, N., Pisignano D., Di Benedetto Francesca, Gigli G., Cingolani R., and Rinaldi R.
RivistaBiomaterials
Volume25
Paginazione1349-1353
ISSN01429612
Parole chiaveantigenicity, article, Atomic force microscopy, Bioassay, Biocompatible, cell culture, Coated materials, Crystallization, Extracellular Matrix Proteins, glass, Immunofluorescence, immunology, Laminin, laminin 1, Materials testing, physiology, priority journal, protein assembly, Protein Conformation, protein determination, Proteins, scleroprotein, Self assembly, structure analysis, Substrates, Supramolecular chemistry, tissue engineering
Abstract

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-100nm 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. © 2003 Elsevier Ltd. All rights reserved.

Note

cited By 39

URLhttps://www.scopus.com/inward/record.uri?eid=2-s2.0-0345256508&doi=10.1016%2fj.biomaterials.2003.08.017&partnerID=40&md5=44dcdd9303b8b13786cabb7645a16cf8
DOI10.1016/j.biomaterials.2003.08.017
Citation KeySgarbi20041349