Abstract
The incorporation of unnatural amino acid into selectable, amplifiable peptide and protein libraries expands the chemical diversity of such libraries, thus considerably facilitating the process of obtaining ligands with improved properties (affinity, specificity, and function), particularly against therapeutically interesting targets. Here, we report that biocytin, a biotin derivative of lysine, can be inserted into an mRNA-protein fusion molecule through amber stop codon suppression. We also demonstrate that templates containing the codon corresponding to the biocytin tRNA (a UAG stop codon) can be enriched by iterative cycles of selection against a streptavidin agarose matrix.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
