Abstract:
:The conformation of single laminin molecules adsorbed on synthetic substrates is directly observed making use of the phase magnitude in tapping mode atomic force microscopy (AFM). With AFM, it is not possible to differentiate the proteins on the substrate if use is made of the height signal, since the roughness of the material becomes of the same order of magnitude as the adsorbed protein, typically 10 nm height. This work shows how AFM can be exploited to reveal protein conformation on polymer materials. Different laminin morphologies are observed on a series of different copolymers based on ethyl acrylate and hydroxyethyl acrylate as a function of the surface density of -OH groups: from globular to completely extended morphologies of the protein molecules are obtained, and the onset of laminin network formation on some substrates can be clearly identified. The results stress the importance of the underlying synthetic substrate's surface chemistry for the biofunctional conformation of adsorbed proteins.
journal_name
Biophys Jjournal_title
Biophysical journalauthors
Rodríguez Hernández JC,Salmerón Sánchez M,Soria JM,Gómez Ribelles JL,Monleón Pradas Mdoi
10.1529/biophysj.106.102491subject
Has Abstractpub_date
2007-07-01 00:00:00pages
202-7issue
1eissn
0006-3495issn
1542-0086pii
biophysj.106.102491journal_volume
93pub_type
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