ArticlePharmaceutical research2018
Light-Induced Covalent Buffer Adducts to Histidine in a Model Protein.
Article in Pharmaceutical research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed, 31 citations in OpenAlex.
- Insights into Photo Degradation and Stabilization Strategies of Antibody-Drug Conjugates with Camptothecin Payloads.Pharmaceutics · 2025Article
- Stability of Protein Pharmaceuticals: Recent Advances.Pharmaceutical research · 2024Review
- Assessing Photostability of mAb Formulations In Situ Using Light-Coupled NMR Spectroscopy.Analytical chemistry · 2024Article
- Primary Processes of Free Radical Formation in Pharmaceutical Formulations of Therapeutic Proteins.Biomolecules · 2023Review
- Photo-Oxidation of Therapeutic Protein Formulations: From Radical Formation to Analytical Techniques.Pharmaceutics · 2021Review
- Light-Induced Histidine Adducts to an IgG1 Molecule Via Oxidized Histidine Residue and the Potential Impact of Polysorbate-20 Concentration.Pharmaceutical research · 2021Article
- Photo-Degradation of Therapeutic Proteins: Mechanistic Aspects.Pharmaceutical research · 2020Review
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
purposeLight is known to induce histidine (His) oxidation and His-His crosslinking in proteins. The crosslinking is resulted from the nucleophilic attack of a His to a photooxidized His from another protein. The goal of this work is to understand if covalent buffer adducts on His residues can be generated by light through similar mechanisms in nucleophilic buffers such as Tris and His.
methodsA model protein (DNase) was buffer exchanged into nucleophilic buffers before light exposure. Photogenerated products were characterized by tryptic peptide mapping with mass spectrometry (MS) analysis. Several buffer adductions on His residues were identified after light exposure. To understand the influencing factors of such reactions, the levels of adducts were measured for six nucleophilic buffers on all His residues in DNase.
resultsThe levels of adducts were found to correlate with the solvent accessibility of the His residue. The levels of adducts also correlate with the structure of the nucleophile, especially the steric restrictions of the nucleophile. The levels of adducts can be higher than that of other His photoreaction products, including photooxidation and crosslinking.
conclusionsIn nucleophilic buffers, light can induce covalently-linked adducts to His residues.
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Registered trials
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