Document Detail


Substrate chemistry-dependent conformations of single laminin molecules on polymer surfaces are revealed by the phase signal of atomic force microscopy.
MedLine Citation:
PMID:  17416620     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Jose Carlos Rodríguez Hernández; Manuel Salmerón Sánchez; José Miguel Soria; José Luis Gómez Ribelles; Manuel Monleón Pradas
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2007-04-06
Journal Detail:
Title:  Biophysical journal     Volume:  93     ISSN:  0006-3495     ISO Abbreviation:  Biophys. J.     Publication Date:  2007 Jul 
Date Detail:
Created Date:  2007-06-07     Completed Date:  2007-08-01     Revised Date:  2013-06-06    
Medline Journal Info:
Nlm Unique ID:  0370626     Medline TA:  Biophys J     Country:  United States    
Other Details:
Languages:  eng     Pagination:  202-7     Citation Subset:  IM    
Affiliation:
Center for Biomaterials, Universidad Politécnica de Valencia, Valencia, Spain.
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MeSH Terms
Descriptor/Qualifier:
Binding Sites
Laminin / chemistry*,  ultrastructure*
Microscopy, Atomic Force / methods*
Polymers / chemistry*
Protein Binding
Protein Conformation
Surface Properties
Chemical
Reg. No./Substance:
0/Laminin; 0/Polymers
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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