Regulating Chemokine-Receptor Interactions through the Site-Specific Bioorthogonal Conjugation of Photoresponsive DNA Strands.

ABSTRACT: Oligonucleotide conjugation has emerged as a versatile molecular tool for regulating protein activity. A state-of-the-art labeling strategy includes the site-specific conjugation of DNA, by employing bioorthogonal groups genetically incorporated in proteins through unnatural amino acids (UAAs). The incorporation of UAAs in chemokines has to date, however, remained underexplored, probably due to their sometimes poor stability following recombinant expression. In this work, we designed a fluorescent stromal-derived factor-1β (SDF-1β) chemokine fusion protein with a bioorthogonal functionality amenable for click reactions. Using amber stop codon suppression, p-azido-_L-phenylalanine was site-specifically incorporated in the fluorescent N-terminal fusion partner, superfolder green fl

SUBMITTER: van Stevendaal MHME 

PROVIDER: S-EPMC10655040 | biostudies-literature | 2023 Nov

REPOSITORIES: biostudies-literature