Camelid single-domain antibody-fragment engineering for (pre)clinical in vivo molecular imaging applications: adjusting the bullet to its target. (September 2013)

• Record Type: Journal Article
• Authors: De Vos, Jens; Devoogdt, Nick; Lahoutte, Tony; Muyldermans, Serge
• Is Part Of: Expert opinion on biological therapy. Volume 13:Number 8(2013:Aug.)
• Page Start: 1149
• Page End: 1160
• Publication Date: 2013-09
• Subjects: Gene therapy -- Periodicals; Protein drugs -- Periodicals; Peptide drugs -- Periodicals; Immunotherapy -- Periodicals; Drug delivery systems -- Periodicals; 615.5
• DOI: 10.1517/14712598.2013.800478
• Languages: English
• ISSNs: 1471-2598

Abstract

<abstract> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold> <italic>Introduction:</italic> </bold> Molecular imaging is a fast developing field and there is a growing need for specific imaging tracers in the clinic. Camelid single-domain antibody-fragments (sdAbs) recently emerged as a new class of molecular imaging tracers.</p> <p> <bold> <italic>Areas covered:</italic> </bold> We review the importance of molecular imaging in the clinic and the use of camelid sdAbs as <italic>in vivo</italic> molecular imaging tracers. Interest in imaging tracers based on antibody fragments or man-made protein scaffolds expanded over the last years. Camelid sdAbs are small, monomeric binding fragments that are derived from unique heavy-chain-only antibodies. <italic>In vivo</italic> imaging studies with sdAbs targeting various cell membrane receptors in different disease models have been reported and more sdAb imaging tracers are under development. The first clinical trial with a camelid sdAb as a molecular imaging tracer targeting the breast cancer marker Human Epidermal growth factor Receptor 2 is currently ongoing.</p> <p> <bold> <italic>Expert opinion:</italic> </bold> We expect that the development and use of sdAbs as tracers for both preclinical and clinical molecular imaging applications will become widespread.</p> </abstract>