TY - JOUR
T1 - Substrate chemistry-dependent conformations of single laminin molecules on polymer surfaces are revealed by the phase signal of atomic force microscopy
AU - Rodríguez Hernández, Jose Carlos
AU - Sánchez, Manuel Salmerón
AU - Soria, José Miguel
AU - Gómez Ribelles, José Luis
AU - Pradas, Manuel Monleón
N1 - Funding Information:
The support of the Universidad Politécnica de Valencia through project No. 5696 and the Spanish Ministry of Science through project No. MAT2006-08120 (including the FEDER financial support) is kindly acknowledged.
PY - 2007/7
Y1 - 2007/7
N2 - 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.
AB - 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.
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U2 - 10.1529/biophysj.106.102491
DO - 10.1529/biophysj.106.102491
M3 - Article
C2 - 17416620
AN - SCOPUS:34447269885
VL - 93
SP - 202
EP - 207
JO - Biophysical Journal
JF - Biophysical Journal
SN - 0006-3495
IS - 1
ER -