TAILIEUCHUNG - Báo cáo khoa học: Synthetic constrained peptide selectively binds and antagonizes death receptor 5

Apoptosis or programmed cell death is an inherent part of the development and homeostasis of multicellular organisms. Dysregulation of apoptosis is implicated in the pathogenesis of diseases such as cancer, neurodegenera-tive diseases and autoimmune disorders. Tumour necrosis factor-related apoptosis-inducing ligand (TRAIL) is able to induce apoptosis by binding death receptor (DR)4 (TRAIL-R1) and DR5 (TRAIL-R2), which makes TRAIL an interesting and promising therapeutic target. | Synthetic constrained peptide selectively binds and antagonizes death receptor 5 InhannQ ri o 11 n If 1 55 t i f ttf1 I-loioQ1 Ri f 55 Cl t r fl i r fl m fl1 F 55 yi f ii yrii2 R I n r t n t ft R l R l 11115511 1 juMaMHd Viieiiiik Iviaiieiie S. neiHo niia Ociiuikiumu Lva szeyezdi iviaiyaiei IVI. Iviuiiaiiy Afshin Samali2 and Wim J. Quax1 1 Department of PharmaceuticalBiology University of Groningen the Netherlands 2 Department of Biochemistry CellStress and Apoptosis Research Group NationalCentre for BiomedicalEngineering Science NationalUniversity of Ireland Galway Ireland Keywords apoptosis DR5 phage display R2C16 TRAIL Correspondence W. J. Quax Department of Pharmaceutical Biology University of Groningen Antonius Deusinglaan 1 9713 AV Groningen the Netherlands Fax 31 50 363 3000 Tel 31 50 363 2558 E-mail These authors contributed equally to this work Received 12 October 2009 revised 17 December 2009 accepted 25 January 2010 doi Apoptosis or programmed cell death is an inherent part of the development and homeostasis of multicellular organisms. Dysregulation of apoptosis is implicated in the pathogenesis of diseases such as cancer neurodegenera-tive diseases and autoimmune disorders. Tumour necrosis factor-related apoptosis-inducing ligand TRAIL is able to induce apoptosis by binding death receptor DR 4 TRAIL-R1 and DR5 TRAIL-R2 which makes TRAIL an interesting and promising therapeutic target. To identify peptides that specifically interact with DR5 a disulfide-constrained phage display peptide library was screened for binders towards this receptor. Phage-displayed peptides were identified that bind specifically to DR5 and not to DR4 nor any of the decoy receptors. We show that the synthesized peptide YCKVILTHRCY in both monomeric and dimeric forms binds specifically to DR5 in such a way that TRAIL binding to DR5 is inhibited. Surface plasmon resonance studies showed higher affinity towards DR5 for the dimeric .

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