Advanced Oxidation Processes in Pharmaceutical Formulations: Photo-Fenton Degradation of Peptides and Proteins
Abstract
:1. Introduction
2. The Photo-Induced Oxidation of Model Peptides in Iron-Containing Citrate Buffer
3. Photo-Induced Formation and Reactions of •CO2− in Iron-Containing Citrate Buffer
4. Photo-Induced Oxidation in the Absence of Added Iron
5. Photo-Induced Oxidation Processes in the Presence of Amino Acids
6. Conclusions and Outlook
Funding
Institutional Review Board Statement
Informed Consent Statement
Data Availability Statement
Conflicts of Interest
References
- Manning, M.C.; Liu, J.; Li, T.; Holcomb, R.E. Rational Design of Liquid Formulations of Proteins. Adv. Protein Chem. Struct. Biol. 2018, 112, 1–59. [Google Scholar] [PubMed]
- Manning, M.C.; Chou, D.K.; Murphy, B.M.; Payne, R.W.; Katayama, D.S. Stability of protein pharmaceuticals: An update. Pharm. Res. 2010, 27, 544–575. [Google Scholar] [CrossRef] [PubMed]
- Davies, K.J. Protein damage and degradation by oxygen radicals. I. general aspects. J. Biol. Chem. 1987, 262, 9895–9901. [Google Scholar] [CrossRef]
- Randolph, T.W.; Schiltz, E.; Sederstrom, D.; Steinmann, D.; Mozziconacci, O.; Schoneich, C.; Freund, E.; Ricci, M.S.; Carpenter, J.F.; Lengsfeld, C.S. Do not drop: Mechanical shock in vials causes cavitation, protein aggregation, and particle formation. J. Pharm. Sci. 2015, 104, 602–611. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Sreedhara, A.; Yin, J.; Joyce, M.; Lau, K.; Wecksler, A.T.; Deperalta, G.; Yi, L.; John Wang, Y.; Kabakoff, B.; Kishore, R.S. Effect of ambient light on IgG1 monoclonal antibodies during drug product processing and development. Eur. J. Pharm. Biopharm. 2016, 100, 38–46. [Google Scholar] [CrossRef]
- Du, C.; Barnett, G.; Borwankar, A.; Lewandowski, A.; Singh, N.; Ghose, S.; Borys, M.; Li, Z.J. Protection of therapeutic antibodies from visible light induced degradation: Use safe light in manufacturing and storage. Eur. J. Pharm. Biopharm. 2018, 127, 37–43. [Google Scholar] [CrossRef]
- Kaiser, W.; Schultz-Fademrecht, T.; Blech, M.; Buske, J.; Garidel, P. Investigating photodegradation of antibodies governed by the light dosage. Int. J. Pharm. 2021, 604, 120723. [Google Scholar] [CrossRef]
- Prajapati, I.; Larson, N.R.; Choudhary, S.; Kalonia, C.; Hudak, S.; Esfandiary, R.; Middaugh, C.R.; Schoneich, C. Visible Light Degradation of a Monoclonal Antibody in a High-Concentration Formulation: Characterization of a Tryptophan-Derived Chromophoric Photo-product by Comparison to Photo-degradation of N-Acetyl-l-tryptophan Amide. Mol. Pharm. 2021, 18, 3223–3234. [Google Scholar] [CrossRef]
- Baertschi, S.W.; Clapham, D.; Foti, C.; Jansen, P.J.; Kristensen, S.; Reed, R.A.; Templeton, A.C.; Tonnesen, H.H. Implications of in-use photostability: Proposed guidance for photostability testing and labeling to support the administration of photosensitive pharmaceutical products, part 1: Drug products administered by injection. J. Pharm. Sci. 2013, 102, 3888–3899. [Google Scholar] [CrossRef]
- Zhang, Z.; Chow, S.Y.; De Guzman, R.; Joh, N.H.; Joubert, M.K.; Richardson, J.; Shah, B.; Wikstrom, M.; Zhou, Z.S.; Wypych, J. A Mass Spectrometric Characterization of Light-Induced Modifications in Therapeutic Proteins. J. Pharm. Sci. 2022, 111, 1556–1564. [Google Scholar] [CrossRef]
- Creed, D. The Photophysics and Photochemistry of the near-uv Absorbing Amino-Acids—I. Tryptophan and Its Simple Derivatives. Photochem. Photobiol. 1984, 39, 537–562. [Google Scholar] [CrossRef]
- Prentice, K.M.; Gillespie, R.; Lewis, N.; Fujimori, K.; McCoy, R.; Bach, J.; Connell-Crowley, L.; Eakin, C.M. Hydroxocobalamin association during cell culture results in pink therapeutic proteins. MAbs 2013, 5, 974–981. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Derfus, G.E.; Dizon-Maspat, J.; Broddrick, J.T.; Velayo, A.C.; Toschi, J.D.; Santuray, R.T.; Hsu, S.K.; Winter, C.M.; Krishnan, R.; Amanullah, A. Red colored IgG4 caused by vitamin B12 from cell culture media combined with disulfide reduction at harvest. MAbs 2014, 6, 679–688. [Google Scholar] [CrossRef] [Green Version]
- Walrant, P.; Santus, R. N-formyl-kynurenine, a tryptophan photooxidation product, as a photodynamic sensitizer. Photochem. Photobiol. 1974, 19, 411–417. [Google Scholar] [CrossRef] [PubMed]
- Reid, L.O.; Vignoni, M.; Martins-Froment, N.; Thomas, A.H.; Dantola, M.L. Photochemistry of tyrosine dimer: When an oxidative lesion of proteins is able to photoinduce further damage. Photochem. Photobiol. Sci. 2019, 18, 1732–1741. [Google Scholar] [CrossRef]
- Dougherty, D.A. Cation-pi interactions in chemistry and biology: A new view of benzene, Phe, Tyr, and Trp. Science 1996, 271, 163–168. [Google Scholar] [CrossRef]
- Dougherty, D.A. The cation-pi interaction. Acc. Chem. Res. 2013, 46, 885–893. [Google Scholar] [CrossRef] [Green Version]
- Juszczak, L.J.; Eisenberg, A.S. The Color of Cation-pi Interactions: Subtleties of Amine-Tryptophan Interaction Energetics Allow for Radical-like Visible Absorbance and Fluorescence. J. Am. Chem. Soc. 2017, 139, 8302–8311. [Google Scholar] [CrossRef]
- Truong, T.B. Charge-Transfer to a Solvent. 2. Luminescence Studies of Tryptophan in Aqueous Solvent at 300-K and 77-K. J. Chem. Phys. 1979, 70, 3536–3543. [Google Scholar] [CrossRef]
- Truong, T.B. Charge-Transfer to a Solvent State. 5. Effect of Solute-Solvent Interaction on the Ionization-Potential of the Solute—Mechanism for Photo-Ionization. J. Phys. Chem. 1980, 84, 964–970. [Google Scholar] [CrossRef]
- Truong, T.B. Charge-Transfer to a Solvent State—Luminescence Studies of Tryptophan in Aqueous 4.5 M CaCl2 Solutions at 300-K and 77-K. J. Phys. Chem. 1980, 84, 960–964. [Google Scholar] [CrossRef]
- Truong, T.B.; Petit, A. Charge-Transfer to Solvent State. 4. Luminescence of Phenol and Tyrosine in Different Aqueous Solvents at 300 and 77-K. J. Phys. Chem. 1979, 83, 1300–1305. [Google Scholar] [CrossRef]
- Subelzu, N.; Schoneich, C. Near UV and Visible Light Induce Iron-Dependent Photodegradation Reactions in Pharmaceutical Buffers: Mechanistic and Product Studies. Mol. Pharm. 2020, 17, 4163–4179. [Google Scholar] [CrossRef]
- Subelzu, N.; Schoneich, C. Pharmaceutical Excipients Enhance Iron-Dependent Photo-Degradation in Pharmaceutical Buffers by near UV and Visible Light: Tyrosine Modification by Reactions of the Antioxidant Methionine in Citrate Buffer. Pharm. Res. 2021, 38, 915–930. [Google Scholar] [CrossRef] [PubMed]
- Prajapati, I.; Subelzu, N.; Zhang, Y.; Wu, Y.; Schoneich, C. Near UV and Visible Light Photo-Degradation Mechanisms in Citrate Buffer: One-Electron Reduction of Peptide and Protein Disulfides promotes Oxidation and Cis/Trans Isomerization of Unsaturated Fatty Acids of Polysorbate 80. J. Pharm. Sci. 2022, 111, 991–1003. [Google Scholar] [CrossRef]
- Ma, D.S.; Yi, H.; Lai, C.; Liu, X.G.; Huo, X.Q.; An, Z.W.; Li, L.; Fu, Y.K.; Li, B.S.; Zhang, M.M.; et al. Critical review of advanced oxidation processes in organic wastewater treatment. Chemosphere 2021, 275, 130104. [Google Scholar] [CrossRef]
- Parvulescu, V.I.; Epron, F.; Garcia, H.; Granger, P. Recent Progress and Prospects in Catalytic Water Treatment. Chem. Rev. 2022, 122, 2981–3121. [Google Scholar] [CrossRef]
- Faust, B.C.; Zepp, R.G. Photochemistry of Aqueous Iron(III) Polycarboxylate Complexes—Roles in the Chemistry of Atmospheric and Surface Waters. Environ. Sci. Technol. 1993, 27, 2517–2522. [Google Scholar] [CrossRef]
- Chen, J.; Browne, W.R. Photochemistry of iron complexes. Coordin. Chem. Rev. 2018, 374, 15–35. [Google Scholar] [CrossRef]
- Wink, D.A.; Nims, R.W.; Saavedra, J.E.; Utermahlen, W.E., Jr.; Ford, P.C. The Fenton oxidation mechanism: Reactivities of biologically relevant substrates with two oxidizing intermediates differ from those predicted for the hydroxyl radical. Proc. Natl. Acad. Sci. USA 1994, 91, 6604–6608. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Ouellette, D.; Alessandri, L.; Piparia, R.; Aikhoje, A.; Chin, A.; Radziejewski, C.; Correia, I. Elevated cleavage of human immunoglobulin gamma molecules containing a lambda light chain mediated by iron and histidine. Anal. Biochem. 2009, 389, 107–117. [Google Scholar] [CrossRef] [PubMed]
- Strickley, R.G.; Lambert, W.J. A review of Formulations of Commercially Available Antibodies. J. Pharm. Sci. 2021, 110, 2590–2608.e56. [Google Scholar] [CrossRef]
- Pozdnyakov, I.P.; Kel, O.V.; Plyusnin, V.F.; Grivin, V.P.; Bazhin, N.M. New insight into photochemistry of ferrioxalate. J. Phys. Chem. A 2008, 112, 8316–8322. [Google Scholar] [CrossRef] [PubMed]
- Butler, J.; Koppenol, W.H.; Margoliash, E. Kinetics and mechanism of the reduction of ferricytochrome c by the superoxide anion. J. Biol. Chem. 1982, 257, 10747–10750. [Google Scholar] [CrossRef]
- Adams, G.E.; Willson, R.L. Pulse Radiolysis Studies on Oxidation of Organic Radicals in Aqueous Solution. J. Chem. Soc. Faraday Trans. 1969, 65, 2981–2987. [Google Scholar] [CrossRef]
- Ilan, Y.; Rabani, J. Some Fundamental Reactions in Radiation-Chemistry—Nanosecond Pulse-Radiolysis. Int. J. Radiat. Phys. Chem. 1976, 8, 609–611. [Google Scholar] [CrossRef]
- Buxton, G.V.; Sellers, R.M.; Mccracken, D.R. Pulse-Radiolysis Study of Monovalent Cadmium, Cobalt, Nickel and Zinc in Aqueous-Solution.2. Reactions of Monovalent Ions. J. Chem. Soc. Faraday Trans. 1 1976, 72, 1464–1476. [Google Scholar] [CrossRef]
- Fojtik, A.; Czapski, G.; Henglein, A. Pulse Radiolytic Investigation of Carboxyl Radical in Aqueous Solution. J. Phys. Chem. 1970, 74, 3204–3208. [Google Scholar] [CrossRef]
- Willson, R.L. Pulse Radiolysis Studies of Electron Transfer in Aqueous Disulphide Solutions. J. Chem. Soc. Chem. Commun. 1970, 1425–1426. [Google Scholar] [CrossRef]
- Favaudon, V.; Tourbez, H.; Houeelevin, C.; Lhoste, J.M. CO2—Radical Induced Cleavage of Disulfide Bonds in Proteins—A Gamma-Ray and Pulse-Radiolysis Mechanistic Investigation. Biochemistry 1990, 29, 10978–10989. [Google Scholar] [CrossRef]
- Joshi, R.; Adhikari, S.; Gopinathan, C.; O’Neill, P. Reduction reactions of bovine serum albumin and lysozyme by CO2—radical in polyvinyl alcohol solution: A pulse radiolysis study. Radiat. Phys. Chem. 1998, 53, 171–176. [Google Scholar] [CrossRef]
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Schöneich, C. Advanced Oxidation Processes in Pharmaceutical Formulations: Photo-Fenton Degradation of Peptides and Proteins. Int. J. Mol. Sci. 2022, 23, 8262. https://doi.org/10.3390/ijms23158262
Schöneich C. Advanced Oxidation Processes in Pharmaceutical Formulations: Photo-Fenton Degradation of Peptides and Proteins. International Journal of Molecular Sciences. 2022; 23(15):8262. https://doi.org/10.3390/ijms23158262
Chicago/Turabian StyleSchöneich, Christian. 2022. "Advanced Oxidation Processes in Pharmaceutical Formulations: Photo-Fenton Degradation of Peptides and Proteins" International Journal of Molecular Sciences 23, no. 15: 8262. https://doi.org/10.3390/ijms23158262