Modulation of the peptide backbone conformation by the selenoxo photoswitch.
Photocontrol of the backbone conformation is a useful step forward in regulating the bioactivities of peptides and proteins by means of external signals. In the present work, the selenium analogue of a peptide bond was introduced into tetrapeptides to obtain surprisingly stable selenoxo peptides. Selenoxo peptide bonds allow for a marked increase of cis content in the photostationary state of peptide chains when irradiated with UV light near 290 nm. Slow thermal re-equilibration with rate constants between 9.9 x 10(-4) and 1.3 x 10(-5) s(-1) shows that the transient nonequilibrium conformations exist long enough to monitor the isomer specificity of biochemical reactions.
Huang
Yun
Y
Max-Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, D-06120 Halle/Saale, Germany.
Jahreis
Günther
G
Lücke
Christian
C
Wildemann
Dirk
D
Fischer
Gunter
G
D010455:Peptides / Q000737:chemistry*; D055668:Photochemical Processes; D011487:Protein Conformation; D018036:Selenium Compounds / Q000737:chemistry*
D010455:Peptides; D018036:Selenium Compounds