A genetic engineering strategy for editing near-infrared-II fluorophores

Rui Tian (), Xin Feng, Long Wei, Daoguo Dai, Ying Ma, Haifeng Pan, Shengxiang Ge, Lang Bai, Chaomin Ke, Yanlin Liu, Lixin Lang, Shoujun Zhu (), Haitao Sun, Yanbao Yu () and Xiaoyuan Chen ()
Additional contact information
Rui Tian: Xiamen University
Xin Feng: Xiamen University
Long Wei: Xiamen University
Daoguo Dai: Xiamen University
Ying Ma: National Institutes of Health (NIH)
Haifeng Pan: Xiamen University
Shengxiang Ge: Xiamen University
Lang Bai: State Key Laboratory of Supramolecular Structure and Materials, College of Chemistry
Chaomin Ke: Xiamen University
Yanlin Liu: Xiamen University
Lixin Lang: National Institutes of Health (NIH)
Shoujun Zhu: State Key Laboratory of Supramolecular Structure and Materials, College of Chemistry
Haitao Sun: School of Physics and Materials Science, East China Normal University
Yanbao Yu: J. Craig Venter Institute, 9714 Medical Center Drive
Xiaoyuan Chen: Yong Loo Lin School of Medicine and Faculty of Engineering, National University of Singapore

Nature Communications, 2022, vol. 13, issue 1, 1-15

Abstract: Abstract The second near-infrared (NIR-II) window is a fundamental modality for deep-tissue in vivo imaging. However, it is challenging to synthesize NIR-II probes with high quantum yields (QYs), good biocompatibility, satisfactory pharmacokinetics, and tunable biological properties. Conventional long-wavelength probes, such as inorganic probes (which often contain heavy metal atoms in their scaffolds) and organic dyes (which contain large π-conjugated groups), exhibit poor biosafety, low QYs, and/or uncontrollable pharmacokinetic properties. Herein, we present a bioengineering strategy that can replace the conventional chemical synthesis methods for generating NIR-II contrast agents. We use a genetic engineering technique to obtain a series of albumin fragments and recombinant proteins containing one or multiple domains that form covalent bonds with chloro-containing cyanine dyes. These albumin variants protect the inserted dyes and remarkably enhance their brightness. The albumin variants can also be genetically edited to develop size-tunable complexes with precisely tailored pharmacokinetics. The proteins can also be conjugated to biofunctional molecules without impacting the complexed dyes. This combination of albumin mutants and clinically-used cyanine dyes can help widen the clinical application prospects of NIR-II fluorophores.

Date: 2022
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DOI: 10.1038/s41467-022-30304-9

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