期刊
NATURE COMMUNICATIONS
卷 13, 期 1, 页码 -出版社
NATURE PORTFOLIO
DOI: 10.1038/s41467-022-30304-9
关键词
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资金
- National Natural Science Foundation of China (NSFC) [82071983]
- National University of Singapore Startup Fund [NUHSRO/2020/133/Startup/08]
- NUS School of Medicine Nanomedicine Translational Research Programme [NUHSRO/2021/034/TRP/09/Nanomedicine]
- National Medical Research Council (NMRC) Centre Grant Programme [CG21APR1005]
The authors propose a strategy to modify protein coatings with biofunctional molecules, resulting in long-wavelength fluorophores for in vivo imaging. These modified albumin variants protect inserted dyes, enhance their brightness, and can be genetically edited to develop size-tunable complexes with precise pharmacokinetics. This approach widens the clinical application prospects for NIR-II fluorophores.
It is currently difficult to synthesise NIR-II probes with good quantum yields, biocompatibility and pharmacokinetics. Here the authors report a strategy to alter these properties by modifying the protein coatings with biofunctional molecules, and generate long-wavelength fluorophores for in vivo imaging. 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 pi-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.
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