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Advances in targeting the folate receptor in the treatment/imaging of cancers

Fernández, Marcos, Javaid, Faiza, Chudasama, Vijay·2018·Chemical Science
DOI 10.1039/c7sc04004kPMC PMC5890329
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Abstract

The folate receptor (FR) is an important biomarker for many cancers, and its overexpression on tumours can be exploited for targeted therapy, diagnosis and imaging.

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Fig. 1 The transformation of healthy epithelial cells to tumour cells and the effect it has on receptor positioning. Upon tumorigenesis, intercellular junctions (tight junctions, adherens junction, desmosomes and gap junctions) are lost and receptors that were previously only found on the apical surface become randomly positioned on the tumour.6
Fig. 1 The transformation of healthy epithelial cells to tumour cells and the effect it has on receptor positioning. Upon tumorigenesis, intercellular junctions (tight junctions, adherens junction, desmosomes and gap junctions) are lost and receptors that were previously only found on the apical surface become randomly positioned on the tumour.6CC BY · PubMed Central
Fig. 2 Structure of folic acid (FA). This vitamin's constituent units are pteroic and glutamic acid.
Fig. 2 Structure of folic acid (FA). This vitamin's constituent units are pteroic and glutamic acid.CC BY · PubMed Central
Fig. 3 Receptor-mediated endocytosis of a folate–drug conjugate. The construct initially binds to FRα or FRβ, forming an invagination and enclosing the conjugate in the early endosome. A mild drop in pH alters the receptor's conformation, resulting in FA–drug detachment. The late endosome's subsequent fusion with the lysosome leads to degradation of the conjugate and release of the free cytotoxic drug into the cell. The recycling endosome delivers the folate receptors back to the cell surface.6
Fig. 3 Receptor-mediated endocytosis of a folate–drug conjugate. The construct initially binds to FRα or FRβ, forming an invagination and enclosing the conjugate in the early endosome. A mild drop in pH alters the receptor's conformation, resulting in FA–drug detachment. The late endosome's subsequent fusion with the lysosome leads to degradation of the conjugate and release of the free cytotoxic drug into the cell. The recycling endosome delivers the folate receptors back to the cell surface.6CC BY · PubMed Central
Fig. 4 Chemical structure of the folic acid-based SMDC vintafolide 1 is comprised of a folate targeting ligand (blue), a peptide spacer (green), a self-immolative disulfide linker (grey) and the potent cytotoxic drug DAVLBH (red).
Fig. 4 Chemical structure of the folic acid-based SMDC vintafolide 1 is comprised of a folate targeting ligand (blue), a peptide spacer (green), a self-immolative disulfide linker (grey) and the potent cytotoxic drug DAVLBH (red).CC BY · PubMed Central
Fig. 5 Mechanism of vintafolide drug release in the intracellular milieu. Glutathione cleaves the disulfide linker and the resulting thiolate undergoes a self-immolative, 1,2-elimination reaction to liberate the free drug DAVLBH.24
Fig. 5 Mechanism of vintafolide drug release in the intracellular milieu. Glutathione cleaves the disulfide linker and the resulting thiolate undergoes a self-immolative, 1,2-elimination reaction to liberate the free drug DAVLBH.24CC BY · PubMed Central
Fig. 6 Structure of the folate–taxoid conjugate 2 developed by Seitz et al.1
Fig. 6 Structure of the folate–taxoid conjugate 2 developed by Seitz et al.1CC BY · PubMed Central
Fig. 7 Enzyme-catalysed double drug release mechanism of β-galactosidase-responsive folate–MMAE conjugate 3.42
Fig. 7 Enzyme-catalysed double drug release mechanism of β-galactosidase-responsive folate–MMAE conjugate 3.42CC BY · PubMed Central
Fig. 8 Structure of the boron complex 10 developed by Gois et al. consisting of (i) a folic acid targeting moiety (blue), (ii) PEG chains and (iii) the cytotoxic agent bortezomib (red).47
Fig. 8 Structure of the boron complex 10 developed by Gois et al. consisting of (i) a folic acid targeting moiety (blue), (ii) PEG chains and (iii) the cytotoxic agent bortezomib (red).47CC BY · PubMed Central
Fig. 9 Proposed mechanism for GluSH-mediated release of bortezomib (15) from complex 11.47
Fig. 9 Proposed mechanism for GluSH-mediated release of bortezomib (15) from complex 11.47CC BY · PubMed Central
Fig. 10 Chemical structure of folate-BODIPY conjugates 16a and 16b.50
Fig. 10 Chemical structure of folate-BODIPY conjugates 16a and 16b.50CC BY · PubMed Central
Fig. 11 Structure of IMGN853 (17). The anti-FRα antibody is conjugated to the DM4 drug via a self-immolative disulfide linker.
Fig. 11 Structure of IMGN853 (17). The anti-FRα antibody is conjugated to the DM4 drug via a self-immolative disulfide linker.CC BY · PubMed Central
Fig. 12 Schematic representation of a NMI-350 nanoemulsion. Difattyacid platins and C6-ceramide are encapsulated in the lipid core and lapidated gadolinium and folate are attached to the surface.21
Fig. 12 Schematic representation of a NMI-350 nanoemulsion. Difattyacid platins and C6-ceramide are encapsulated in the lipid core and lapidated gadolinium and folate are attached to the surface.21CC BY · PubMed Central
Fig. 13 Structure of the difattyacid cisplatins 18a–18c and the DPSE-PEG3400-FA spacer 19.
Fig. 13 Structure of the difattyacid cisplatins 18a–18c and the DPSE-PEG3400-FA spacer 19.CC BY · PubMed Central
Fig. 14 Nanotube formation from nanosheets.65
Fig. 14 Nanotube formation from nanosheets.65CC BY · PubMed Central
Fig. 15 Chemical structure of 99mTc-etarfolatide.
Fig. 15 Chemical structure of 99mTc-etarfolatide.CC BY · PubMed Central
Fig. 16 Chemical structures of albumin-binding folate conjugates cm09, cm10 and rf42. They are each composed of three modules: (i) folic acid for FRα-expressing tumour targeting (blue), (ii) an albumin-binding moiety (pink), and (iii) the chelator (green) (DOTA for cm09 and cm10 and NODAGA for rf42) for coordination of 68Ga or 64Cu. The three functionalities are connected via a lysine linker in radiofolates cm10 and rf42, and by a triazole linker in the case of conjugate cm09.22,82,85
Fig. 16 Chemical structures of albumin-binding folate conjugates cm09, cm10 and rf42. They are each composed of three modules: (i) folic acid for FRα-expressing tumour targeting (blue), (ii) an albumin-binding moiety (pink), and (iii) the chelator (green) (DOTA for cm09 and cm10 and NODAGA for rf42) for coordination of 68Ga or 64Cu. The three functionalities are connected via a lysine linker in radiofolates cm10 and rf42, and by a triazole linker in the case of conjugate cm09.22,82,85CC BY · PubMed Central
Fig. 17 Fluorescence off-on response of nanoprobe in FRα-positive cell.91
Fig. 17 Fluorescence off-on response of nanoprobe in FRα-positive cell.91CC BY · PubMed Central
Marcos Fernández
Marcos FernándezCC BY · PubMed Central
Faiza Javaid
Faiza JavaidCC BY · PubMed Central
Vijay Chudasama
Vijay ChudasamaCC BY · PubMed Central

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Metadata

Authors
Fernández, M., Javaid, F., & Chudasama, V.
Affiliations
Department of Chemistry
ORCID
Chudasama, Vijay
Venue
Chemical Science
Publisher
Royal Society of Chemistry (RSC)
Published
2018
Volume
9
Issue
4
Pages
790-810
ISSN
  • 2041-6520
  • 2041-6539
DOI
10.1039/c7sc04004k
PMC
PMC5890329
Cited by
539
References
0
Language
en
Licence
creativecommons.org/licenses/by/3.0/ (vor)

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