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Structure-based mutagenesis of phycobiliprotein smURFP for optoacoustic imaging.

ACS Chem. Biol. 14, 1896-1903 (2019)
Postprint DOI
Open Access Green
Photo- or optoacoustics (OA) imaging is increasingly being used as a non-invasive imaging method that can simultaneously reveal structure and function in deep tissue. However, the most frequent transgenic OA labels are current fluorescent proteins that are not optimized for OA imaging. Thus, they lack OA signal strength, and their absorption maxima are positioned at short wavelengths, thus giving small penetration depths and strong background signals. Here, we apply insights from our recent determination of the structure of the fluorescent phycobiliprotein smURFP to mutate a range of residues to promote the nonradiative decay pathway that generates the OA signal. We identified hydrophobic and aromatic substitutions within the chromophore-binding pocket that substantially increase the intensity of the OA signal and red-shift the absorption. Our results demonstrate the feasibility of structure-based mutagenesis to repurpose fluorescent probes for OA imaging, and they may provide structure-function insights for de novo engineering of transgenic OA probes.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter Infrared Fluorescent Proteins; Photoacoustic Tomography; Biliverdin; Binding; Bilirubin
ISSN (print) / ISBN 1554-8929
e-ISSN 1554-8937
Zeitschrift ACS Chemical Biology
Quellenangaben Band: 14, Heft: 9, Seiten: 1896-1903 Artikelnummer: , Supplement: ,
Verlag American Chemical Society (ACS)
Verlagsort Washington
Begutachtungsstatus Peer reviewed