Phosphorylation state-responsive lanthanide peptide conjugates: a luminescence switch based on reversible complex reorganization.
[reaction: see text] A luminogenic probe for peptide dephosphorylation has been developed. It consists of a serine-/tyrosine-containing peptide modified on the N-terminus with a tryptophan residue and a DTPA chelate capable of binding Tb(3+). We propose a mechanistic model for the luminescence enhancement based on the interconversion of monomeric and dimeric lanthanide species, which is affected by the phosphorylation state of the serine or tyrosine residue. The optical switch reports effectively on phosphatase-catalyzed dephosphorylation in vitro.
Tremblay
Matthew S
MS
Department of Chemistry, Columbia University, New York, New York 10027, USA.
Zhu
Qing
Q
Martí
Angel A
AA
Dyer
Joanne
J
Halim
Marlin
M
Jockusch
Steffen
S
Turro
Nicholas J
NJ
Sames
Dalibor
D
D000469:Alkaline Phosphatase / Q000378:metabolism*; D000595:Amino Acid Sequence; D028581:Lanthanoid Series Elements / Q000737:chemistry*; D049449:Luminescence; D008163:Luminescent Measurements / Q000379:methods; D008958:Models, Molecular; D004369:Pentetic Acid / Q000737:chemistry; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry* / Q000378:metabolism; D010766:Phosphorylation; D012694:Serine / Q000737:chemistry; D013725:Terbium / Q000737:chemistry; D014364:Tryptophan / Q000737:chemistry
D028581:Lanthanoid Series Elements; D010455:Peptides; D013725:Terbium; D012694:Serine; D004369:Pentetic Acid; D014364:Tryptophan; D000469:Alkaline Phosphatase