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Structure-based mutagenesis of phycobiliprotein smURFP for optoacoustic imaging.
ACS Chem. Biol. 14, 1896-1903 (2019)
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
Verlag
American Chemical Society (ACS)
Verlagsort
Washington
Nichtpatentliteratur
Publikationen
Begutachtungsstatus
Peer reviewed