Photochromic Fluorescent Probe Strategy for the Super-resolution Imaging of Biologically Important Biomarkers

Here, we report a β-galactosidase (β-Gal)-responsive photochromic fluorescent probe, NpG, that was designed to prebind to human serum albumin (HSA) to form the probe/protein hybrid, NpG@HSA. The formation of NpG@HSA led to an increase in fluorescence emission (520 nm) corresponding to the binding of...

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Published inJournal of the American Chemical Society Vol. 142; no. 42; pp. 18005 - 18013
Main Authors Chai, Xianzhi, Han, Hai-Hao, Sedgwick, Adam C, Li, Na, Zang, Yi, James, Tony D, Zhang, Junji, Hu, Xi-Le, Yu, Yang, Li, Yao, Wang, Yan, Li, Jia, He, Xiao-Peng, Tian, He
Format Journal Article
LanguageEnglish
Published WASHINGTON American Chemical Society 21.10.2020
Amer Chemical Soc
Subjects
beta-Galactosidase - analysis
beta-Galactosidase - metabolism
biomarkers
Biomarkers - analysis
Biomarkers - metabolism
Cell Line
Chemistry
Chemistry, Multidisciplinary
fluorescence
fluorescent dyes
Fluorescent Dyes - chemical synthesis
Fluorescent Dyes - chemistry
galactose
human serum albumin
Humans
hybrids
microscopy
Microscopy, Confocal
Molecular Structure
Optical Imaging
permeability
Photochemical Processes
photoisomerization
photostability
phototoxicity
Physical Sciences
Science & Technology
Serum Albumin, Human - chemistry
solubility
CELLS
NANOPARTICLES
FLUOROPHORES
BETA-GALACTOSIDASE
POSTTRANSLATIONAL MODIFICATIONS
SENESCENCE
IONIZING-RADIATION
INTRAMOLECULAR SPIROCYCLIZATION
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Abstract Here, we report a β-galactosidase (β-Gal)-responsive photochromic fluorescent probe, NpG, that was designed to prebind to human serum albumin (HSA) to form the probe/protein hybrid, NpG@HSA. The formation of NpG@HSA led to an increase in fluorescence emission (520 nm) corresponding to the binding of the fluorescent naphthalimide unit with HSA. In addition, this enabled visualization of the spiropyran fluorescence emission in aqueous media. Our probe/protein hybrid approach afforded a unique imaging platform with enhanced cell permeability and solubility that was capable of visualizing the cellular uptake of NpG@HSA before its activation by β-Gal. The β-Gal-mediated cleavage of the galactose unit within the NpG@HSA hybrid resulted in the formation of NpM@HSA and an increase in red fluorescence emission (620 nm). The resultant merocyanine unit was then able to undergo photoisomerization (merocyanine ↔ spiropyran) to facilitate STORM (i.e., stochastic optical reconstruction microscopy) imaging with minimal phototoxicity and excellent photostability/reversibility. Using STORM, NpG@HSA was able to determine the subcellular distribution of β-Gal activity between cell lines with nanoscale precision. We believe that this system represents a versatile imaging platform for the design of photochromic fluorescent probes suitable for illuminating the precise location of disease-specific biomarkers in various cellular processes.
AbstractList Here, we report a beta-galactosidase (beta-Gal)-responsive photochromic fluorescent probe, NpG, that was designed to prebind to human serum albumin (HSA) to form the probe/protein hybrid, NpG@HSA. The formation of NpG@HSA led to an increase in fluorescence emission (520 nm) corresponding to the binding of the fluorescent naphthalimide unit with HSA. In addition, this enabled visualization of the spiropyran fluorescence emission in aqueous media. Our probe/protein hybrid approach afforded a unique imaging platform with enhanced cell permeability and solubility that was capable of visualizing the cellular uptake of NpG@HSA before its activation by beta-Gal. The beta-Gal-mediated cleavage of the galactose unit within the NpG@HSA hybrid resulted in the formation of NpM@HSA and an increase in red fluorescence emission (620 nm). The resultant merocyanine unit was then able to undergo photoisomerization (merocyanine <-> spiropyran) to facilitate STORM (i.e., stochastic optical reconstruction microscopy) imaging with minimal phototoxicity and excellent photostability/reversibility. Using STORM, NpG@HSA was able to determine the subcellular distribution of beta-Gal activity between cell lines with nanoscale precision. We believe that this system represents a versatile imaging platform for the design of photochromic fluorescent probes suitable for illuminating the precise location of disease-specific biomarkers in various cellular processes.
Here, we report a β-galactosidase (β-Gal)-responsive photochromic fluorescent probe, NpG, that was designed to prebind to human serum albumin (HSA) to form the probe/protein hybrid, NpG@HSA. The formation of NpG@HSA led to an increase in fluorescence emission (520 nm) corresponding to the binding of the fluorescent naphthalimide unit with HSA. In addition, this enabled visualization of the spiropyran fluorescence emission in aqueous media. Our probe/protein hybrid approach afforded a unique imaging platform with enhanced cell permeability and solubility that was capable of visualizing the cellular uptake of NpG@HSA before its activation by β-Gal. The β-Gal-mediated cleavage of the galactose unit within the NpG@HSA hybrid resulted in the formation of NpM@HSA and an increase in red fluorescence emission (620 nm). The resultant merocyanine unit was then able to undergo photoisomerization (merocyanine ↔ spiropyran) to facilitate STORM (i.e., stochastic optical reconstruction microscopy) imaging with minimal phototoxicity and excellent photostability/reversibility. Using STORM, NpG@HSA was able to determine the subcellular distribution of β-Gal activity between cell lines with nanoscale precision. We believe that this system represents a versatile imaging platform for the design of photochromic fluorescent probes suitable for illuminating the precise location of disease-specific biomarkers in various cellular processes.
Here, we report a β-galactosidase (β-Gal)-responsive photochromic fluorescent probe, , that was designed to prebind to human serum albumin (HSA) to form the probe/protein hybrid, . The formation of led to an increase in fluorescence emission (520 nm) corresponding to the binding of the fluorescent naphthalimide unit with HSA. In addition, this enabled visualization of the spiropyran fluorescence emission in aqueous media. Our probe/protein hybrid approach afforded a unique imaging platform with enhanced cell permeability and solubility that was capable of visualizing the cellular uptake of before its activation by β-Gal. The β-Gal-mediated cleavage of the galactose unit within the hybrid resulted in the formation of and an increase in red fluorescence emission (620 nm). The resultant merocyanine unit was then able to undergo photoisomerization (merocyanine ↔ spiropyran) to facilitate STORM (i.e., stochastic optical reconstruction microscopy) imaging with minimal phototoxicity and excellent photostability/reversibility. Using STORM, was able to determine the subcellular distribution of β-Gal activity between cell lines with nanoscale precision. We believe that this system represents a versatile imaging platform for the design of photochromic fluorescent probes suitable for illuminating the precise location of disease-specific biomarkers in various cellular processes.
Here, we report a β-galactosidase (β-Gal)-responsive photochromic fluorescent probe, NpG, that was designed to prebind to human serum albumin (HSA) to form the probe/protein hybrid, NpG@HSA. The formation of NpG@HSA led to an increase in fluorescence emission (520 nm) corresponding to the binding of the fluorescent naphthalimide unit with HSA. In addition, this enabled visualization of the spiropyran fluorescence emission in aqueous media. Our probe/protein hybrid approach afforded a unique imaging platform with enhanced cell permeability and solubility that was capable of visualizing the cellular uptake of NpG@HSA before its activation by β-Gal. The β-Gal-mediated cleavage of the galactose unit within the NpG@HSA hybrid resulted in the formation of NpM@HSA and an increase in red fluorescence emission (620 nm). The resultant merocyanine unit was then able to undergo photoisomerization (merocyanine ↔ spiropyran) to facilitate STORM (i.e., stochastic optical reconstruction microscopy) imaging with minimal phototoxicity and excellent photostability/reversibility. Using STORM, NpG@HSA was able to determine the subcellular distribution of β-Gal activity between cell lines with nanoscale precision. We believe that this system represents a versatile imaging platform for the design of photochromic fluorescent probes suitable for illuminating the precise location of disease-specific biomarkers in various cellular processes.Here, we report a β-galactosidase (β-Gal)-responsive photochromic fluorescent probe, NpG, that was designed to prebind to human serum albumin (HSA) to form the probe/protein hybrid, NpG@HSA. The formation of NpG@HSA led to an increase in fluorescence emission (520 nm) corresponding to the binding of the fluorescent naphthalimide unit with HSA. In addition, this enabled visualization of the spiropyran fluorescence emission in aqueous media. Our probe/protein hybrid approach afforded a unique imaging platform with enhanced cell permeability and solubility that was capable of visualizing the cellular uptake of NpG@HSA before its activation by β-Gal. The β-Gal-mediated cleavage of the galactose unit within the NpG@HSA hybrid resulted in the formation of NpM@HSA and an increase in red fluorescence emission (620 nm). The resultant merocyanine unit was then able to undergo photoisomerization (merocyanine ↔ spiropyran) to facilitate STORM (i.e., stochastic optical reconstruction microscopy) imaging with minimal phototoxicity and excellent photostability/reversibility. Using STORM, NpG@HSA was able to determine the subcellular distribution of β-Gal activity between cell lines with nanoscale precision. We believe that this system represents a versatile imaging platform for the design of photochromic fluorescent probes suitable for illuminating the precise location of disease-specific biomarkers in various cellular processes.
Author Li, Na
Han, Hai-Hao
Zhang, Junji
Hu, Xi-Le
Tian, He
James, Tony D
Wang, Yan
Yu, Yang
Li, Jia
Li, Yao
Sedgwick, Adam C
Chai, Xianzhi
Zang, Yi
He, Xiao-Peng
AuthorAffiliation National Center for Drug Screening, State Key Laboratory of Drug Research
Department of Chemistry
National Center for Protein Science Shanghai
Key Laboratory for Advanced Materials and Joint International Research Laboratory of Precision Chemistry and Molecular Engineering, Feringa Nobel Prize Scientist Joint Research Center, School of Chemistry and Molecular Engineering, Frontiers Center for Materiobiology and Dynamic Chemistry
AuthorAffiliation_xml – name: Department of Chemistry
– name: Key Laboratory for Advanced Materials and Joint International Research Laboratory of Precision Chemistry and Molecular Engineering, Feringa Nobel Prize Scientist Joint Research Center, School of Chemistry and Molecular Engineering, Frontiers Center for Materiobiology and Dynamic Chemistry
– name: National Center for Protein Science Shanghai
– name: National Center for Drug Screening, State Key Laboratory of Drug Research
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  givenname: Xianzhi
  surname: Chai
  fullname: Chai, Xianzhi
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– sequence: 2
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  surname: Han
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  organization: National Center for Drug Screening, State Key Laboratory of Drug Research
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  givenname: Adam C
  orcidid: 0000-0002-3132-2913
  surname: Sedgwick
  fullname: Sedgwick, Adam C
  organization: Department of Chemistry
– sequence: 4
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  orcidid: 0000-0002-8476-511X
  surname: Li
  fullname: Li, Na
  organization: National Center for Protein Science Shanghai
– sequence: 5
  givenname: Yi
  surname: Zang
  fullname: Zang, Yi
  organization: National Center for Drug Screening, State Key Laboratory of Drug Research
– sequence: 6
  givenname: Tony D
  orcidid: 0000-0002-4095-2191
  surname: James
  fullname: James, Tony D
  organization: Department of Chemistry
– sequence: 7
  givenname: Junji
  orcidid: 0000-0003-2823-4637
  surname: Zhang
  fullname: Zhang, Junji
  email: zhangjunji@ecust.edu.cn
  organization: Key Laboratory for Advanced Materials and Joint International Research Laboratory of Precision Chemistry and Molecular Engineering, Feringa Nobel Prize Scientist Joint Research Center, School of Chemistry and Molecular Engineering, Frontiers Center for Materiobiology and Dynamic Chemistry
– sequence: 8
  givenname: Xi-Le
  surname: Hu
  fullname: Hu, Xi-Le
  organization: Key Laboratory for Advanced Materials and Joint International Research Laboratory of Precision Chemistry and Molecular Engineering, Feringa Nobel Prize Scientist Joint Research Center, School of Chemistry and Molecular Engineering, Frontiers Center for Materiobiology and Dynamic Chemistry
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  surname: Yu
  fullname: Yu, Yang
  organization: National Center for Protein Science Shanghai
– sequence: 10
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  surname: Li
  fullname: Li, Yao
  organization: National Center for Protein Science Shanghai
– sequence: 11
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  surname: Wang
  fullname: Wang, Yan
  organization: National Center for Protein Science Shanghai
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  givenname: Jia
  surname: Li
  fullname: Li, Jia
  email: jli@simm.ac.cn
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  orcidid: 0000-0002-8736-3511
  surname: He
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  surname: Tian
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/32955867$$D View this record in MEDLINE/PubMed
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Issue 42
Keywords CELLS
NANOPARTICLES
FLUOROPHORES
BETA-GALACTOSIDASE
POSTTRANSLATIONAL MODIFICATIONS
SENESCENCE
IONIZING-RADIATION
INTRAMOLECULAR SPIROCYCLIZATION
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Snippet Here, we report a β-galactosidase (β-Gal)-responsive photochromic fluorescent probe, NpG, that was designed to prebind to human serum albumin (HSA) to form the...
Here, we report a beta-galactosidase (beta-Gal)-responsive photochromic fluorescent probe, NpG, that was designed to prebind to human serum albumin (HSA) to...
Here, we report a β-galactosidase (β-Gal)-responsive photochromic fluorescent probe, , that was designed to prebind to human serum albumin (HSA) to form the...
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SubjectTerms beta-Galactosidase - analysis
beta-Galactosidase - metabolism
biomarkers
Biomarkers - analysis
Biomarkers - metabolism
Cell Line
Chemistry
Chemistry, Multidisciplinary
fluorescence
fluorescent dyes
Fluorescent Dyes - chemical synthesis
Fluorescent Dyes - chemistry
galactose
human serum albumin
Humans
hybrids
microscopy
Microscopy, Confocal
Molecular Structure
Optical Imaging
permeability
Photochemical Processes
photoisomerization
photostability
phototoxicity
Physical Sciences
Science & Technology
Serum Albumin, Human - chemistry
solubility
Title Photochromic Fluorescent Probe Strategy for the Super-resolution Imaging of Biologically Important Biomarkers
URI http://dx.doi.org/10.1021/jacs.0c05379
http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=Summon&SrcAuth=ProQuest&DestApp=WOS&DestLinkType=FullRecord&UT=000580559000024
https://www.ncbi.nlm.nih.gov/pubmed/32955867
https://www.proquest.com/docview/2444882815
https://www.proquest.com/docview/2524302007
Volume 142
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