Conformation of Microcontact-Printed Proteins by Atomic Force Microscopy Molecular Sizing

We investigated the structural changes occurring in proteins patterned via microcontact printing. This was done by molecular sizing using atomic force microscopy to observe the structure of printed individual metalloprotein molecules in the unlabeled and untreated states. We observed that the size o...

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Bibliographic Details
Published in:Langmuir 2005-05, Vol.21 (11), p.5154-5158
Main Authors: Biasco, Adriana, Pisignano, Dario, Krebs, Blandine, Pompa, Pier Paolo, Persano, Luana, Cingolani, Roberto, Rinaldi, Ross
Format: Article
Language:English
Subjects:
Adsorption
Azurin - chemistry
Chemistry
Exact sciences and technology
General and physical chemistry
Microscopy, Atomic Force - methods
Particle Size
Protein Conformation
Pseudomonas aeruginosa - chemistry
Sensitivity and Specificity
Silicon Dioxide - chemistry
Surface physical chemistry
Surface Properties
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Summary:We investigated the structural changes occurring in proteins patterned via microcontact printing. This was done by molecular sizing using atomic force microscopy to observe the structure of printed individual metalloprotein molecules in the unlabeled and untreated states. We observed that the size of the printed proteins were more than 2-fold smaller than the native shape, which indicates that some deformations take place upon the contact-assisted adsorption on silanized silicon dioxide. This can be attributed to simultaneously occurring effects, and particularly to the sandwiching between surfaces of very different hydrophilic/hydrophobic properties during contact lithography.
ISSN:0743-7463
1520-5827
DOI:10.1021/la050010j