Systematic Investigation of EDC/sNHS-Mediated Bioconjugation Reactions for Carboxylated Peptide Substrates
Autor: | Kyle A. Totaro, Bradley L. Pentelute, Keshab Bhattacharya, Sa V. Ho, Jennifer Marie Thorn, Jari I. Finneman, Xiaoli Liao, Mark A. Massa, Justin B. Sperry |
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Rok vydání: | 2016 |
Předmět: |
Biomedical Engineering
Pharmaceutical Science Bioengineering Peptide Nanotechnology 02 engineering and technology 010402 general chemistry 01 natural sciences Substrate Specificity chemistry.chemical_compound Nucleophile Product formation Chromatography High Pressure Liquid Carbodiimide Pharmacology chemistry.chemical_classification Bioconjugation Organic Chemistry 021001 nanoscience & nanotechnology Combinatorial chemistry 0104 chemical sciences Carbodiimides chemistry Reagent Substrate specificity Amine gas treating Peptides 0210 nano-technology Biotechnology |
Zdroj: | Bioconjugate Chemistry. 27:994-1004 |
ISSN: | 1520-4812 1043-1802 |
Popis: | 1-Ethyl-3-(3-(dimethylamino)propyl)carbodiimide (EDC) bioconjugations have been utilized in preparing variants for medical research. While there have been advances in optimizing the reaction for aqueous applications, there has been limited focus toward identifying conditions and side reactions that interfere with product formation. We present a systematic investigation of EDC/N-hydroxysulfosuccinimide (sNHS)-mediated bioconjugations on carboxylated peptides and small proteins. We identified yet-to-be-reported side products arising from both the reagents and substrates. Model peptides used in this study illustrate particular substrates are more susceptible to side reactions than others. From our studies, we found that bioconjugations are more efficient with high concentrations of amine nucleophile but not sNHS. Performing bioconjugations on a model affibody protein show that the trends established with model peptides hold for more complex systems. |
Databáze: | OpenAIRE |
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