Shading the TRF2 recruiting function: a new horizon in drug development.
The shelterin protein TRF2 has come to the limelight for its role in telomere maintenance and tumorigenesis. Herein, the application of rational design and synthesis allowed identifying the first TRF2TRFH binder able to elicit a marked DNA damage response in cancer cells. This work paves the way for the unprecedented employment of a chemical tool to finely tune specific mechanisms underlying telomere maintenance.
DiSTABiF, Second University of Naples , Caserta, Italy.
Salvatore
S
Di Maro
Pasquale
P
Zizza
Erica
E
Salvati
Viviana
V
De Luca
Clemente
C
Capasso
Iolanda
I
Fotticchia
Bruno
B
Pagano
Luciana
L
Marinelli
Eric
E
Gilson
Ettore
E
Novellino
Sandro
S
Cosconati
Annamaria
A
Biroccio
D015195:Drug Design; D006801:Humans; D008958:Models, Molecular; D010456:Peptides, Cyclic / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology*; D035341:Telomeric Repeat Binding Protein 2 / Q000037:antagonists & inhibitors* / Q000378:metabolism
D010456:Peptides, Cyclic; C504753:TERF2 protein, human; D035341:Telomeric Repeat Binding Protein 2