Abstract
The atomic force microscope (AFM) is widely used in biological sciences due to its ability to perform imaging experiments at high resolution in a physiological environment, without special sample preparation such as fixation or staining. AFM is unique, in that it allows single molecule information of mechanical properties and molecular recognition to be gathered. This review sets out to identify methodological applications of AFM for characterization of fiber-forming proteins and peptides. The basics of AFM operation are detailed, with in-depth information for any life scientist to get a grasp on AFM capabilities. It also briefly describes antibody recognition imaging and mapping of nanomechanical properties on biological samples. Subsequently, examples of AFM application to fiber-forming natural proteins, and fiberforming synthetic peptides are given. Here, AFM is used primarily for structural characterization of fibers in combination with other techniques, such as circular dichroism and fluorescence spectroscopy. More recent developments in antibody recognition imaging to identify constituents of protein fibers formed in human disease are explored. This review, as a whole, seeks to encourage the life scientists dealing with protein aggregation phenomena to consider AFM as a part of their research toolkit, by highlighting the manifold capabilities of this technique.
Keywords: Atomic force microscopy, antibody-recognition imaging, protein aggregation, peptide fibers, AFM, CM, tapping mode, friction channel records, hydrophobic forces, cantilever deflection
Current Protein & Peptide Science
Title:Characterization of Fiber-Forming Peptides and Proteins by Means of Atomic Force Microscopy
Volume: 13 Issue: 3
Author(s): Rhiannon G. Creasey, Christopher T. Gibson and Nicolas H. Voelcker
Affiliation:
Keywords: Atomic force microscopy, antibody-recognition imaging, protein aggregation, peptide fibers, AFM, CM, tapping mode, friction channel records, hydrophobic forces, cantilever deflection
Abstract: The atomic force microscope (AFM) is widely used in biological sciences due to its ability to perform imaging experiments at high resolution in a physiological environment, without special sample preparation such as fixation or staining. AFM is unique, in that it allows single molecule information of mechanical properties and molecular recognition to be gathered. This review sets out to identify methodological applications of AFM for characterization of fiber-forming proteins and peptides. The basics of AFM operation are detailed, with in-depth information for any life scientist to get a grasp on AFM capabilities. It also briefly describes antibody recognition imaging and mapping of nanomechanical properties on biological samples. Subsequently, examples of AFM application to fiber-forming natural proteins, and fiberforming synthetic peptides are given. Here, AFM is used primarily for structural characterization of fibers in combination with other techniques, such as circular dichroism and fluorescence spectroscopy. More recent developments in antibody recognition imaging to identify constituents of protein fibers formed in human disease are explored. This review, as a whole, seeks to encourage the life scientists dealing with protein aggregation phenomena to consider AFM as a part of their research toolkit, by highlighting the manifold capabilities of this technique.
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Cite this article as:
G. Creasey Rhiannon, T. Gibson Christopher and H. Voelcker Nicolas, Characterization of Fiber-Forming Peptides and Proteins by Means of Atomic Force Microscopy, Current Protein & Peptide Science 2012; 13 (3) . https://dx.doi.org/10.2174/138920312800785058
DOI https://dx.doi.org/10.2174/138920312800785058 |
Print ISSN 1389-2037 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5550 |
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