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BIM – Stapled BH3 Peptide

Cancer Research Peptide

BIM apoptotic peptide is derived from the BH3 domain of the pro-apoptotic Bcl-2 family member BIM. As a stabilized α-helical peptide, it is designed to mimic the native BH3 helix and disrupt anti-apoptotic Bcl-2 family protein interactions. By binding to Bcl-2, Bcl-xL, and related survival proteins, this peptide promotes mitochondrial apoptotic signaling.

Disease Target 

Primarily used in cancer research targeting malignancies characterized by dysregulated apoptosis, including leukemias, lymphomas, and solid tumors with overexpression of anti-apoptotic Bcl-2 family proteins. By mimicking the BH3 domain of BIM, this peptide reactivates apoptotic signaling in apoptosis-resistant cancer cells.

Stapling Strategy 

BIM is synthesized using Fmoc-(S)-2-(4-pentenyl)alanine (Fmoc-(S5)-OH, CAS: 288617-73-2), incorporated at i,i+4 positions within the BH3 sequence during solid-phase peptide synthesis (SPPS). A ruthenium-catalyzed ring-closing olefin metathesis reaction generates the (CH₂)₄ hydrocarbon staple, stabilizing the α-helical conformation and enhancing cellular permeability and proteolytic stability.

 

Technical specification

KD20 peptide Sequency :
EIWIAQELR(S5)IGD(S5)FNAYYA-NH2
KD20 peptide MW : 2421.75 g/mol
KD20 peptide Purity : > 95%
KD20 peptide Counter-Ion : TFA Salts
Peptide library synthesis KD20 peptide Delivery format : Lyophilized

Price

 

Product Size Price €
 Price $
SB331-1mg 1 mg 651 781
SB331-5mg 5 mg 825 990
SB331-10mg 10 mg 1109 1331

 

For more information about stapled peptides, please visit our dedicated page.

Explore our Stapled Peptide Catalog products. Click HERE to discover additional reference compounds.

A fluorescent FAM-labeled version of this peptide is available for imaging and uptake studies. Tap the button below to view the FAM-conjugated product.

View FAM-Labeled Version

Custom Stapled Peptide Services

If your target is not listed, we offer custom stapled peptide design and synthesis. Whether you require sequence optimization, specific modifications, or larger production quantities, our team can support your project. Submit your project details and we will provide a personalized proposal.

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References

Nat Commun 11, 3301 (2020). https://doi.org/10.1038/s41467-020-17074-y

Characterization of an alternative BAK-binding site for BH3 peptides

Abstract

Many cellular stresses are transduced into apoptotic signals through modification or up-regulation of the BH3-only subfamily of BCL2 proteins. Through direct or indirect mechanisms, these proteins activate BAK and BAX to permeabilize the mitochondrial outer membrane. While the BH3-only proteins BIM, PUMA, and tBID have been confirmed to directly activate BAK through its canonical BH3 binding groove, whether the BH3-only proteins BMF, HRK or BIK can directly activate BAK is less clear. Here we show that BMF and HRK bind and directly activate BAK. Through NMR studies, site-directed mutagenesis, and advanced molecular dynamics simulations, we also find that BAK activation by BMF and possibly HRK involves a previously unrecognized binding groove formed by BAK α4, α6, and α7 helices. Alterations in this groove decrease the ability of BMF and HRK to bind BAK, permeabilize membranes and induce apoptosis, suggesting a potential role for this BH3-binding site in BAK activation.

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