The anti-apoptotic factor Bcl-2 is over-expressed in B-cell lymphoma cells as their main survival mechanism by binding to IP3R2 on the endoplasmic reticulum (ER).  In this study, a cell-penetrating version of the BIRD-2 peptide (Bcl-2/IP3R Disrupter-2 peptide with a TAT sequence) made by LifeTein was used to break up the complex formed by Bcl-2 and IP3R2 in human diffuse large B-cell lymphoma (DLBCL) cells. Ca²⁺ signaling-related events are suggested to be the killing mechanism of BIRD-2 peptide on DLBCL cells.

BIRD-2, a peptide that specifically disrupts the Bcl2/IP3R complex, was utilized to further verify the mitochondrial Ca²⁺ regulatory mechanism via the Bmal1-Bcl2/IP3R signaling pathway. It was found that BIRD-2 aggravated mitochondrial Ca²⁺ overload and apoptosis in vitro.

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BIRD-2 peptide (sequence: RKKRRQRRRGGNVYTEIKCNSLLPLAAIVRV) was purchased from LifeTein (South Plainfield, NJ, USA) with a purity of >85%.

Bird-2 Peptides & B-Cell Lymphoma

Reference:

BIRD-2 peptide (LifeTein, USA), specifically disrupting the Bcl2/IP3R complex, was used in HGHP-treated H9c2 cells for 12 h (20 μM)

Inhibiting Bcl-2 via its BH4 domain in DLBCL cancers to provoke pro-apoptotic Ca²⁺ signaling

BIRD-2, a BH4-domain-targeting peptide of Bcl-2, provokes Bax/Bak-independent cell death in B-cell cancers through mitochondrial Ca2+-dependent mPTP opening

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