Photoreactive Stapled BH3 Peptides to Dissect the BCL-2 Family Interactome

被引：35

作者：

Braun, Craig R. ^{[1
,2
,3
]}

Mintseris, Julian ^{[4
,5
]}

Gavathiotis, Evripidis ^{[1
,2
,3
]}

Bird, Gregory H. ^{[1
,2
,3
]}

Gygi, Steven P. ^{[4
,5
]}

Walensky, Loren D. ^{[1
,2
,3
]}

机构：

[1] Harvard Univ, Sch Med, Dana Farber Canc Inst, Dept Pediat Oncol, Boston, MA 02115 USA

[2] Harvard Univ, Sch Med, Childrens Hosp Boston, Boston, MA 02115 USA

[3] Dana Farber Canc Inst, Program Canc Chem Biol, Boston, MA 02115 USA

[4] Harvard Univ, Sch Med, Dept Cell Biol, Boston, MA 02115 USA

[5] Harvard Univ, Sch Med, Taplin Biol Mass Spectrometry Facil, Boston, MA 02115 USA

来源：

CHEMISTRY & BIOLOGY | 2010年 / 17卷 / 12期

关键词：

PROTEIN STRUCTURES; DOCKING APPROACH; BAX; ACTIVATION; PROTEOMICS; APOPTOSIS; DOMAINS; HELIX; NMR; INHIBITOR;

D O I：

10.1016/j.chembiol.2010.09.015

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Defining protein interactions forms the basis for discovery of biological pathways, disease mechanisms, and opportunities for therapeutic intervention. To harness the robust binding affinity and selectivity of structured peptides for interactome discovery, we engineered photoreactive stapled BH3 peptide helices that covalently capture their physiologic BCL-2 family targets. The crosslinking alpha helices covalently trap both static and dynamic protein interactors, and enable rapid identification of interaction sites, providing a critical link between interactome discovery and targeted drug design.

引用

页码：1325 / 1333

页数：9

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