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[1]J. M. Astle, D. G. Udugamasooriya, J. E. Smallshaw & T. Kodadek; A VEGFR2 Antagonist and Other Peptoids Evade Immune Recognition. Int. J. Pept. Res. Ther. 14, 223-227 (2008)
[2]Y.-U. Kwon & T. Kodadek; Quantitative evaluation of the relative cell permeability of peptoids and peptides. J. Am. Chem. Soc. 129, 1508-1509 (2007)
[3]R. J. Simon, et al.; Peptoids: a modular approach to drug discovery. Proc. Natl. Acad. Sci. U. S. A. 89, 9367-9371 (1992)
[4]R. N. Zuckermann, J. M. Kerr, S. B. H. Kent & W. H. Moos; Efficient method for the preparation of peptoids (oligo(N-substituted glycines)) by submonomer solid-phase synthesis. J. Am. Chem. Soc. 114, 10646-10647 (1992)
[5]T. Uno, E. Beausoleil, R. A. Goldsmith, B. H. Levine & R. N. Zuckermann New submonomers for poly N-substituted glycines (peptoids) Tetrahedron Lett. 40, 1475-1478 (1999)
[6]S. L. Seurynck-Servoss, M. T. Dohm & A. E. Barron; Effects of including an N-terminal insertion region and arginine-mimetic side chains in helical peptoid analogues of lung surfactant protein B. Biochemistry (Mosc.) 45, 11809-11818 (2006)
[7]H. L. Bolt & S. L. Cobb; A practical method for the synthesis of peptoids containing both lysine-type and arginine-type monomers. Org Biomol Chem 14, 1211-1215 (2016)
[8]P. A. Wender et al.; The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: peptoid molecular transporters. Proc. Natl. Acad. Sci. U. S. A. 97, 13003-13008 (2000)
[9]E. J. Robertson et al.; Design, Synthesis, Assembly, and Engineering of Peptoid Nanosheets. Acc. Chem. Res. 49, 379-389 (2016)
[10]G. L. Butterfoss, P. D. Renfrew, B. Kuhlman, K. Kirshenbaum & R. A. Bonneau; Preliminary survey of the peptoid folding landscape. J. Am. Chem. Soc. 131, 16798-16807 (2009)
[11]C. Baldauf, R. Günther & H.-J. Hofmann; Helices in peptoids of alpha- and beta-peptides. Phys. Biol. 3, S1-9 (2006)
[12]A. R. Statz et al.; Experimental and theoretical investigation of chain length and surface coverage on fouling of surface grafted polypeptoids. Biointerphases 4, FA22-FA32
[13]T. S. Burkoth, A. T. Fafarman, D. H. Charych, M. D. Connolly & R. N. Zuckermann; Incorporation of unprotected heterocyclic side chains into peptoid oligomers via solid-phase submonomer synthesis. J. Am. Chem. Soc. 125, 8841-8845 (2003)
[14]T. Hjelmgaard et al. Convenient solution-phase synthesis and conformational studies of novel linear and cyclic alpha,beta-alternating peptoids. Org. Lett. 11, 4100-4103 (2009)
[15]L. A. Wessjohann, D. G. Rivera & O. E. Vercillo; Multiple multicomponent macrocyclizations (MiBs): a strategic development toward macrocycle diversity. Chem. Rev. 109, 796-814 (2009)
[16]B.-C. Lee, R. N. Zuckermann & K. A. Dill; Folding a nonbiological polymer into a compact multihelical structure. J. Am. Chem. Soc. 127, 10999-11009 (2005)
[17]B.-C. Lee, T. K. Chu, K. A. Dill & R. N. Zuckermann; Biomimetic nanostructures: creating a high-affinity zinc-binding site in a folded nonbiological polymer. J. Am. Chem. Soc. 130, 8847-8855 (2008)
[18]L. M. De León-Rodríguez et al.; MRI detection of VEGFR2 in vivo using a low molecular weight peptoid-(Gd)8-dendron for targeting. J. Am. Chem. Soc. 132, 12829-12831 (2010)
[19]W. Cai & H. Hong; Peptoid and Positron Emission Tomography: an Appealing Combination. Am. J. Nucl. Med. Mol. Imaging 1, 76 (2011)
[20]G. Hao, A. Hajibeigi, L. M. D. León-Rodríguez, O. K. Oz & X. Sun; Peptoid-based PET imaging of vascular endothelial growth factor receptor (VEGFR) expression. Am. J. Nucl. Med. Mol. Imaging 1, 65-75 (2011)
[21]S. T. A. Passos, J. R. Correa, S. L. M. Soares, W. A. da Silva & B. A. D. Neto; Fluorescent Peptoids as Selective Live Cell Imaging Probes. J. Org. Chem. 81, 2646-2651 (2016)
[22]Q. Hu et al.; Elevated cleaved caspase-3 is associated with shortened overall survival in several cancer types. Int. J. Clin. Exp. Pathol. 7, 5057-5070 (2014)
[23]A. M. Pérez-López, M. L. Soria-Gila, E. R. Marsden, A. Lilienkampf & M. Bradley; Fluorogenic Substrates for In situ Monitoring of Caspase-3 Activity in Live Cells. PLOS ONE 11, e0153209 (2016)
[24]A. Furka, F. Sebestyén, M. Asgedom & G. Dibó; General method for rapid synthesis of multicomponent peptide mixtures. Int. J. Pept. Protein Res. 37, 487-493 (1991)
[25]K. S. Lam et al.; A new type of synthetic peptide library for identifying ligand-binding activity. Nature 354, 82-84 (1991)
[26]P. Alluri, B. Liu, P. Yu, X. Xiao & T. Kodadek; Isolation and characterization of coactivator-binding peptoids from a combinatorial library. Mol. Bio. syst. 2, 568-579 (2006)
[27]T. Kodadek & K. Bachhawat-Sikder; Optimized protocols for the isolation of specific protein-binding peptides or peptoids from combinatorial libraries displayed on beads. Mol. Bio. syst. 2, 25-35 (2006)
[28]R. N. Zuckermann & T. Kodadek; Peptoids as potential therapeutics. Curr. Opin. Mol. Ther. 11, 299-307 (2009)
[29]W. Huang et al.; Learning from host-defense peptides: cationic, amphipathic peptoids with potent anticancer activity. PloS One 9, e90397 (2014)
[30]J. C. Hooks, J. P. Matharage & D. G. Udugamasooriya; Development of homomultimers and heteromultimers of lung cancer-specific peptoids. Biopolymers 96, 567-577 (2011)
[31]J. Lee, W. Huang, J. M. Broering, A. E. Barron & J. Seo; Prostate tumor specific peptide-peptoid hybrid prodrugs. Bioorg. Med. Chem. Lett. 25, 2849-2852 (2015)
[32]J. M. Matharage, J. D.Minna, R. A. Brekken & D. G. Udugamasooriya; Unbiased Selection of Peptide–Peptoid Hybrids Specific for Lung Cancer Compared to Normal Lung Epithelial Cells. ACS Chem. Biol. 10, 2891-2899 (2015)
[33]T. J. Desai, J. E. Toombs, J. D. Minna, R. A. Brekken & D. G. Udugamasooriya; Identification of lipid-phosphatidylserine (PS) as the target of unbiasedly selected cancer specific peptide-peptoid hybrid PPS1. Oncotarget (2016)
[34]G. Selivanova; p53: Fighting Cancer. Curr. Cancer Drug Targets 4, 385-402 (2004)
[35]P. A. J. Muller & K. H. Vousden; Mutant p53 in Cancer: New Functions and Therapeutic Opportunities. Cancer Cell 25, 304-317 (2014)
[36]T. Hara, S. R. Durell, M. C. Myers & D. H. Appella; Probing the Structural Requirements of Peptoids That Inhibit HDM2−p53 Interactions. J. Am. Chem. Soc. 128, 1995-2004 (2006)
[37]J. A. Fresno Vara et al.; PI3K/Akt signaling pathway and cancer. Cancer Treat. Rev. 30, 193-204 (2004)
[38]Y. Tal-Gan, N. S. Freeman, S. Klein, A. Levitzki, & C. Gilon; Synthesis and structure-activity relationship studies of peptidomimetic PKB/Akt inhibitors: the significance of backbone interactions. Bioorg. Med. Chem. 18, 2976-2985 (2010)
[39]D. G. Udugamasooriya, S. P. Dineen, R. A. Brekken, & T. A. Kodadek; peptoid ‘antibody surrogate’ that antagonizes VEGF receptor 2 activity. J. Am. Chem. Soc. 130, 5744-5752 (2008)
[40]D. Diedrich et al.; Rational design and diversity-oriented synthesis of peptoid-based selective HDAC6 inhibitors. Chem. Commun. 52, 3219-3222 (2016)
[41]M. D. Shortridge & G. Varani; Structure based approaches for targeting non-coding RNAs with small molecules. Curr Opin Struct Biol. 30, 79-88 (2015)
[42]F. A. Abulwerdi, & J. S. Schneekloth Jr.; Microarray-based technologies for the discovery of selective, RNA-binding molecules. Methods
[43]L. P. Labuda, A. Pushechnikov & M. D. Disney; Small molecule microarrays of RNA-focused peptoids help identify inhibitors of a pathogenic group I intron. ACS Chem. Biol. 4, 299-307 (2009)
[44]S. Chirayil, R. Chirayil & K. J. Luebke; Discovering ligands for a microRNA precursor with peptoid microarrays. Nucleic Acids Res. 37, 5486-5497 (2009)
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Frontiers in Bioscience-Elite (FBE) is published by IMR Press from Volume 13 Issue 2 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on imrpress.com as a courtesy and upon agreement with Frontiers in Bioscience.
1 Signal Transduction in Cancer and Stem Cells Laboratory, Division of Cancer Biology and Inflammatory Disorder, Council of Scientific and Industrial Research-Indian Institute of Chemical Biology (CSIR-IICB), 4 Raja S.C. Mullick Road Kolkata- 700032 and CN-06 Setor-V, Salt Lake, Kolkata-700091, India
2 Department of Microbiology, Barrackpore Rastraguru Surendranath College, 6 Riverside Road and 85 Middle Road, Barrackpore, Kolkata-700 120, India
*Author to whom correspondence should be addressed.
Abstract
Genetic variations in cancer cells are the underpinning for the development of resistance and failure of the treatment by current anticancer drugs. Thus, an ideal drug must overcome failure of treatment and prevents development of drug resistance. There are a wide variety of emerging, easy to prepare and cost effective group of drugs that are collectively called peptoids or peptidomimetics. These new set of drugs exhibit distinct features including protease resistance, are non-immunogenic, do not hinder functionality and backbone polarity, and can adopt different conformations. These drugs have shown promise as diagnostic and therapeutic tools in a wide variety of diseases. Here, we discuss the recent advancement in the design and synthesis of peptoids and use of these drugs in the diganosis and treatment of a wide number of cancers of the lung, prostate, and breast.
Keywords
- Peptoid
- Cancer
- Therapy
- Diagnosis
- Review
References
- [1] J. M. Astle, D. G. Udugamasooriya, J. E. Smallshaw & T. Kodadek; A VEGFR2 Antagonist and Other Peptoids Evade Immune Recognition. Int. J. Pept. Res. Ther. 14, 223-227 (2008)Cited within: 0Google Scholar
- [2] Y.-U. Kwon & T. Kodadek; Quantitative evaluation of the relative cell permeability of peptoids and peptides. J. Am. Chem. Soc. 129, 1508-1509 (2007)Cited within: 0Google Scholar
- [3] R. J. Simon, et al.; Peptoids: a modular approach to drug discovery. Proc. Natl. Acad. Sci. U. S. A. 89, 9367-9371 (1992)
- [4] R. N. Zuckermann, J. M. Kerr, S. B. H. Kent & W. H. Moos; Efficient method for the preparation of peptoids (oligo(N-substituted glycines)) by submonomer solid-phase synthesis. J. Am. Chem. Soc. 114, 10646-10647 (1992)Cited within: 0Google Scholar
- [5] T. Uno, E. Beausoleil, R. A. Goldsmith, B. H. Levine & R. N. Zuckermann New submonomers for poly N-substituted glycines (peptoids) Tetrahedron Lett. 40, 1475-1478 (1999)Cited within: 0Google Scholar
- [6] S. L. Seurynck-Servoss, M. T. Dohm & A. E. Barron; Effects of including an N-terminal insertion region and arginine-mimetic side chains in helical peptoid analogues of lung surfactant protein B. Biochemistry (Mosc.) 45, 11809-11818 (2006)Cited within: 0Google Scholar
- [7] H. L. Bolt & S. L. Cobb; A practical method for the synthesis of peptoids containing both lysine-type and arginine-type monomers. Org Biomol Chem 14, 1211-1215 (2016)Cited within: 0Google Scholar
- [8] P. A. Wender et al.; The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: peptoid molecular transporters. Proc. Natl. Acad. Sci. U. S. A. 97, 13003-13008 (2000)
- [9] E. J. Robertson et al.; Design, Synthesis, Assembly, and Engineering of Peptoid Nanosheets. Acc. Chem. Res. 49, 379-389 (2016)
- [10] G. L. Butterfoss, P. D. Renfrew, B. Kuhlman, K. Kirshenbaum & R. A. Bonneau; Preliminary survey of the peptoid folding landscape. J. Am. Chem. Soc. 131, 16798-16807 (2009)Cited within: 0Google Scholar
- [11] C. Baldauf, R. Günther & H.-J. Hofmann; Helices in peptoids of alpha- and beta-peptides. Phys. Biol. 3, S1-9 (2006)Cited within: 0Google Scholar
- [12] A. R. Statz et al.; Experimental and theoretical investigation of chain length and surface coverage on fouling of surface grafted polypeptoids. Biointerphases 4, FA22-FA32
- [13] T. S. Burkoth, A. T. Fafarman, D. H. Charych, M. D. Connolly & R. N. Zuckermann; Incorporation of unprotected heterocyclic side chains into peptoid oligomers via solid-phase submonomer synthesis. J. Am. Chem. Soc. 125, 8841-8845 (2003)Cited within: 0Google Scholar
- [14] T. Hjelmgaard et al. Convenient solution-phase synthesis and conformational studies of novel linear and cyclic alpha,beta-alternating peptoids. Org. Lett. 11, 4100-4103 (2009)
- [15] L. A. Wessjohann, D. G. Rivera & O. E. Vercillo; Multiple multicomponent macrocyclizations (MiBs): a strategic development toward macrocycle diversity. Chem. Rev. 109, 796-814 (2009)Cited within: 0Google Scholar
- [16] B.-C. Lee, R. N. Zuckermann & K. A. Dill; Folding a nonbiological polymer into a compact multihelical structure. J. Am. Chem. Soc. 127, 10999-11009 (2005)Cited within: 0Google Scholar
- [17] B.-C. Lee, T. K. Chu, K. A. Dill & R. N. Zuckermann; Biomimetic nanostructures: creating a high-affinity zinc-binding site in a folded nonbiological polymer. J. Am. Chem. Soc. 130, 8847-8855 (2008)Cited within: 0Google Scholar
- [18] L. M. De León-Rodríguez et al.; MRI detection of VEGFR2 in vivo using a low molecular weight peptoid-(Gd)8-dendron for targeting. J. Am. Chem. Soc. 132, 12829-12831 (2010)
- [19] W. Cai & H. Hong; Peptoid and Positron Emission Tomography: an Appealing Combination. Am. J. Nucl. Med. Mol. Imaging 1, 76 (2011)
- [20] G. Hao, A. Hajibeigi, L. M. D. León-Rodríguez, O. K. Oz & X. Sun; Peptoid-based PET imaging of vascular endothelial growth factor receptor (VEGFR) expression. Am. J. Nucl. Med. Mol. Imaging 1, 65-75 (2011)Cited within: 0Google Scholar
- [21] S. T. A. Passos, J. R. Correa, S. L. M. Soares, W. A. da Silva & B. A. D. Neto; Fluorescent Peptoids as Selective Live Cell Imaging Probes. J. Org. Chem. 81, 2646-2651 (2016)Cited within: 0Google Scholar
- [22] Q. Hu et al.; Elevated cleaved caspase-3 is associated with shortened overall survival in several cancer types. Int. J. Clin. Exp. Pathol. 7, 5057-5070 (2014)
- [23] A. M. Pérez-López, M. L. Soria-Gila, E. R. Marsden, A. Lilienkampf & M. Bradley; Fluorogenic Substrates for In situ Monitoring of Caspase-3 Activity in Live Cells. PLOS ONE 11, e0153209 (2016)Cited within: 0Google Scholar
- [24] A. Furka, F. Sebestyén, M. Asgedom & G. Dibó; General method for rapid synthesis of multicomponent peptide mixtures. Int. J. Pept. Protein Res. 37, 487-493 (1991)Cited within: 0Google Scholar
- [25] K. S. Lam et al.; A new type of synthetic peptide library for identifying ligand-binding activity. Nature 354, 82-84 (1991)
- [26] P. Alluri, B. Liu, P. Yu, X. Xiao & T. Kodadek; Isolation and characterization of coactivator-binding peptoids from a combinatorial library. Mol. Bio. syst. 2, 568-579 (2006)Cited within: 0Google Scholar
- [27] T. Kodadek & K. Bachhawat-Sikder; Optimized protocols for the isolation of specific protein-binding peptides or peptoids from combinatorial libraries displayed on beads. Mol. Bio. syst. 2, 25-35 (2006)
- [28] R. N. Zuckermann & T. Kodadek; Peptoids as potential therapeutics. Curr. Opin. Mol. Ther. 11, 299-307 (2009)Cited within: 0Google Scholar
- [29] W. Huang et al.; Learning from host-defense peptides: cationic, amphipathic peptoids with potent anticancer activity. PloS One 9, e90397 (2014)
- [30] J. C. Hooks, J. P. Matharage & D. G. Udugamasooriya; Development of homomultimers and heteromultimers of lung cancer-specific peptoids. Biopolymers 96, 567-577 (2011)Cited within: 0Google Scholar
- [31] J. Lee, W. Huang, J. M. Broering, A. E. Barron & J. Seo; Prostate tumor specific peptide-peptoid hybrid prodrugs. Bioorg. Med. Chem. Lett. 25, 2849-2852 (2015)Cited within: 0Google Scholar
- [32] J. M. Matharage, J. D.Minna, R. A. Brekken & D. G. Udugamasooriya; Unbiased Selection of Peptide–Peptoid Hybrids Specific for Lung Cancer Compared to Normal Lung Epithelial Cells. ACS Chem. Biol. 10, 2891-2899 (2015)Cited within: 0Google Scholar
- [33] T. J. Desai, J. E. Toombs, J. D. Minna, R. A. Brekken & D. G. Udugamasooriya; Identification of lipid-phosphatidylserine (PS) as the target of unbiasedly selected cancer specific peptide-peptoid hybrid PPS1. Oncotarget (2016)Cited within: 0Google Scholar
- [34] G. Selivanova; p53: Fighting Cancer. Curr. Cancer Drug Targets 4, 385-402 (2004)
- [35] P. A. J. Muller & K. H. Vousden; Mutant p53 in Cancer: New Functions and Therapeutic Opportunities. Cancer Cell 25, 304-317 (2014)Cited within: 0Google Scholar
- [36] T. Hara, S. R. Durell, M. C. Myers & D. H. Appella; Probing the Structural Requirements of Peptoids That Inhibit HDM2−p53 Interactions. J. Am. Chem. Soc. 128, 1995-2004 (2006)Cited within: 0Google Scholar
- [37] J. A. Fresno Vara et al.; PI3K/Akt signaling pathway and cancer. Cancer Treat. Rev. 30, 193-204 (2004)
- [38] Y. Tal-Gan, N. S. Freeman, S. Klein, A. Levitzki, & C. Gilon; Synthesis and structure-activity relationship studies of peptidomimetic PKB/Akt inhibitors: the significance of backbone interactions. Bioorg. Med. Chem. 18, 2976-2985 (2010)Cited within: 0Google Scholar
- [39] D. G. Udugamasooriya, S. P. Dineen, R. A. Brekken, & T. A. Kodadek; peptoid ‘antibody surrogate’ that antagonizes VEGF receptor 2 activity. J. Am. Chem. Soc. 130, 5744-5752 (2008)Cited within: 0Google Scholar
- [40] D. Diedrich et al.; Rational design and diversity-oriented synthesis of peptoid-based selective HDAC6 inhibitors. Chem. Commun. 52, 3219-3222 (2016)
- [41] M. D. Shortridge & G. Varani; Structure based approaches for targeting non-coding RNAs with small molecules. Curr Opin Struct Biol. 30, 79-88 (2015)Cited within: 0Google Scholar
- [42] F. A. Abulwerdi, & J. S. Schneekloth Jr.; Microarray-based technologies for the discovery of selective, RNA-binding molecules. MethodsCited within: 0Google Scholar
- [43] L. P. Labuda, A. Pushechnikov & M. D. Disney; Small molecule microarrays of RNA-focused peptoids help identify inhibitors of a pathogenic group I intron. ACS Chem. Biol. 4, 299-307 (2009)Cited within: 0Google Scholar
- [44] S. Chirayil, R. Chirayil & K. J. Luebke; Discovering ligands for a microRNA precursor with peptoid microarrays. Nucleic Acids Res. 37, 5486-5497 (2009)Cited within: 0Google Scholar
