Characterization of fiber-forming peptides and proteins by means of atomic force microscopy

Rhiannon Creasey, Christopher Gibson, Nicolas Voelcker

    Research output: Contribution to journalArticlepeer-review

    10 Citations (Scopus)


    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.

    Original languageEnglish
    Pages (from-to)232-257
    Number of pages26
    JournalCurrent Protein and Peptide Science
    Issue number3
    Publication statusPublished - May 2012


    • Antibody-recognition imaging
    • Atomic force microscopy
    • Peptide fibers
    • Protein aggregation


    Dive into the research topics of 'Characterization of fiber-forming peptides and proteins by means of atomic force microscopy'. Together they form a unique fingerprint.

    Cite this