BIRD-2 peptide

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.

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 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 the BIRD-2 peptide on DLBCL cells.

BIRD-2 peptide is a 31-residue synthetic peptide with the sequence Arg-Lys-Lys-Arg-Arg-Gln-Arg-Arg-Arg-Gly-Gly-Asn-Val-Tyr-Thr-Glu-Ile-Lys-Cys-Asn-Ser-Leu-Leu-Pro-Leu-Ala-Ala-Ile-Val-Arg-Val. The sequence contains 1 cysteine residue, allowing thiol/disulfide chemistry when available; contains 3 Lys and 7 Arg residues, contributing cationic character. These sequence-derived properties describe the reagent chemically; no specific biological activity is assigned without product-specific experimental evidence.

• thiol-selective conjugation or immobilization studies
• LC-MS/HPLC analytical method development
• sequence-specific assay controls

Sequence-derived chemical properties support reagent selection and experimental planning but do not establish biological function. Solubility, aggregation, adsorption, conjugation efficiency, and assay performance should be validated under the intended conditions.