Intramolecular bridges formed by photoswitchable click amino acids

• Christian Hoppmann,
• Ronald Kühne and
• Michael Beyermann

Beilstein J. Org. Chem. 2012, 8, 884–889, doi:10.3762/bjoc.8.100

• ; isomerization; molecular switches; photoswitchable click amino acid; thiol–ene click; Introduction Photoswitchable bridges that are site-specifically incorporated into proteins allow the conformation and activity of proteins to be modulated by light. In contrast to common bivalent thiol reactive azobenzene

• structured domains, which may influence the intramolecular thiol click reaction between the PSCaa and a cysteine residue. Here, we show that the thiol click reaction of the photoswitchable click amino acid (PSCaa) at the i,i+4 position and a cysteine in a helical model peptide, under structure-inducing

• , thus lending itself to an application in vivo in combination with protein synthesis with ad hoc evolved orthogonal tRNA/synthease pairs in an ongoing project [10]. Experimental The photoswitchable click amino acid 2-amino-3-(4-((3-vinylphenyl)diazenyl)phenyl)propanoic acid (PSCaa) and the helical model