期刊
BIOCONJUGATE CHEMISTRY
卷 19, 期 1, 页码 153-157出版社
AMER CHEMICAL SOC
DOI: 10.1021/bc700231v
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- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM072700] Funding Source: NIH RePORTER
- NIGMS NIH HHS [GM072700-01] Funding Source: Medline
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.
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