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Methyleneation of peptides by N, N, N, N -tetramethylethylenediamine (TEMED) under conditions used for free radical polymerization: A mechanistic study
- Source :
- Shirangi, M, Sastre Toraño, J, Sellergren, B, Hennink, W E, Somsen, G W & Van Nostrum, C F 2015, ' Methyleneation of peptides by N, N, N, N-tetramethylethylenediamine (TEMED) under conditions used for free radical polymerization : A mechanistic study ', Bioconjugate chemistry, vol. 26, no. 1, pp. 90-100 . https://doi.org/10.1021/bc500445d, Bioconjugate Chemistry, 26(1), 90. American Chemical Society : Division of Carbohydrate Chemistry, Bioconjugate chemistry, 26(1), 90-100. American Chemical Society
- Publication Year :
- 2015
-
Abstract
- Free radical polymerization is often used to prepare protein and peptide-loaded hydrogels for the design of controlled release systems and molecular imprinting materials. Peroxodisulfates (ammonium peroxodisulfates (APS) or potassium peroxodisulfates (KPS)) with N,N,N,N-tetramethylethylenediamine (TEMED) are frequently used as initiator and catalyst. However, exposure to these free radical polymerization reagents may lead to modification of the protein and peptide. In this work, we show the modification of lysine residues by ammonium peroxodisulfate (APS)/TEMED of the immunostimulant thymopentin (TP5). Parallel studies on a decapeptide and a library of 15 dipeptides were performed to reveal the mechanism of modification. LC-MS of APS/TEMED-exposed TP5 revealed a major reaction product with an increased mass (+12 Da) with respect to TP5. LC-MS2 and LC-MS3 were performed to obtain structural information on the modified peptide and localize the actual modification site. Interpretation of the obtained data demonstrates the formation of a methylene bridge between the lysine and arginine residue in the presence of TEMED, while replacing TEMED with a sodium bisulfite catalyst did not show this modification. Studies with the other peptides showed that the TEMED radical can induce methyleneation on peptides when lysine is next to arginine, proline, cysteine, aspargine, glutamine, histidine, tyrosine, tryptophan, and aspartic acid residues. Stability of peptides and protein needs to be considered when using APS/TEMED in in situ polymerization systems. The use of an alternative catalyst such as sodium bisulfite may preserve the chemical integrity of peptides during in situ polymerization.
- Subjects :
- Free Radicals
Radical polymerization
Lysine
Biomedical Engineering
Pharmaceutical Science
Peptide
Bioengineering
Polymerization
chemistry.chemical_compound
Residue (chemistry)
Peptide Library
Taverne
Organic chemistry
Amino Acid Sequence
In situ polymerization
chemistry.chemical_classification
Pharmacology
Protein Stability
Chemistry
Organic Chemistry
Tetramethylethylenediamine
Ethylenediamines
Combinatorial chemistry
Molecular Weight
Ammonium Sulfate
Sodium bisulfite
Peptides
SDG 6 - Clean Water and Sanitation
Biotechnology
Subjects
Details
- Language :
- English
- ISSN :
- 10431802
- Database :
- OpenAIRE
- Journal :
- Shirangi, M, Sastre Toraño, J, Sellergren, B, Hennink, W E, Somsen, G W & Van Nostrum, C F 2015, ' Methyleneation of peptides by N, N, N, N-tetramethylethylenediamine (TEMED) under conditions used for free radical polymerization : A mechanistic study ', Bioconjugate chemistry, vol. 26, no. 1, pp. 90-100 . https://doi.org/10.1021/bc500445d, Bioconjugate Chemistry, 26(1), 90. American Chemical Society : Division of Carbohydrate Chemistry, Bioconjugate chemistry, 26(1), 90-100. American Chemical Society
- Accession number :
- edsair.doi.dedup.....7233dbeed2e5151b50b15ff08e40c3eb