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BIM (FAM)

Cancer Research Peptide

This FAM-labeled Bim apoptotic peptide is derived from the BH3 domain of the pro-apoptotic Bcl-2 family member BIM. As a hydrocarbon-stapled 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 anti-apoptotic proteins, this peptide promotes mitochondrial apoptotic signaling and caspase activation. The hydrocarbon staple enhances α-helicity, proteolytic stability, and cellular permeability compared to the linear BH3 sequence. The N-terminal FAM label (Ex/Em = 495/520 nm) is attached via an Ahx spacer (6-aminohexanoic acid, CAS: 60-32-2). This flexible linker reduces steric interference between the fluorophore and the peptide backbone, ensuring optimal binding and accurate cellular imaging.

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 (FAM) 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. The N‑terminal FAM label (Ex/Em = 495/520 nm) is introduced via an Ahx spacer, using 6‑aminohexanoic acid (Ahx, CAS: 60‑32‑2) as a flexible linker to separate the fluorophore from the peptide backbone, thereby minimizing steric interference and preserving the peptide’s binding and structural properties. This design enables fluorescence‑based cellular uptake and localization studies.

 

Technical specification

KD20 peptide Sequency : FAM-Ahx-EIWIAQELR(S5)IGD(S5)FNAYYA
KD20 peptide MW : 2921.26 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 $
SB332-1mg 1 mg 791 921
SB332-5mg 5 mg 965 1130
SB332-10mg 10 mg 1249 1471

 

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

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

An unlabeled version of this peptide is available for applications not requiring fluorescence. Tap the button below to view the non-conjugated product.

View Unlabeled 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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