Attachment of Peptide Building Blocks to Proteins Through Tyrosine Bioconjugation
| Autor: | Dante W. Romanini, Matthew B. Francis |
|---|---|
| Rok vydání: | 2007 |
| Předmět: |
Spectrometry
Mass Electrospray Ionization Immunoblotting Lysine Biomedical Engineering Pharmaceutical Science Bioengineering Peptide Mannich Bases Residue (chemistry) Formaldehyde Immunoblot Analysis Amino Acid Sequence Tyrosine Pharmacology chemistry.chemical_classification Bioconjugation Organic Chemistry Proteins Chymotrypsinogen Amino acid chemistry Biochemistry Peptides Biotechnology Cysteine |
| Zdroj: | Bioconjugate Chemistry. 19:153-157 |
| ISSN: | 1520-4812 1043-1802 |
| DOI: | 10.1021/bc700231v |
| Popis: | Recent efforts have yielded a number of short peptide sequences with useful binding, sensing, and cellular uptake properties. In order to attach these sequences to tyrosine residues on intact proteins, a three-component Mannich-type strategy is reported. Two solid phase synthetic routes were developed to access peptides up to 20 residues in length with anilines at either the N- or C-termini. In the presence of 20 mM formaldehyde, these functional groups were coupled to tyrosine residues on proteins under mild reaction conditions. The identities of the resulting bioconjugates were confirmed using mass spectrometry and immunoblot analysis. Screening experiments have demonstrated that the method is compatible with substrates containing all of the amino acids, including lysine and cysteine residues. Importantly, tyrosine residues on proteins exhibit much faster reaction rates, allowing short peptides containing this residue to be coupled without cross reactions. |
| Databáze: | OpenAIRE |
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