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Bcl-2 Binding Peptide, cell permeable

* Please kindly note that our products are not to be used for therapeutic purposes and cannot be sold to patients.

It is a peptide that binds to Bcl-2 with high affinity. It is derived from the BH3 domain (a death domain) of Bad, amino acid residues 140 to 165, and is cellular permeable due to the N-terminal modification by a decanoyl moiety.

Category

Functional Peptides

Catalog number

BAT-013325

Molecular Formula

C153H240N44O42S

Molecular Weight

3399.93

Specification
Reference Reading

IUPAC Name

(2S)-2-[[2-[[(2S)-6-amino-2-[[(2S)-2-[[(2S)-2-[[2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[2-[[(2S)-2-[[(2S)-2-[[(2S)-5-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-4-amino-2-[[(2S)-6-amino-2-(decanoylamino)hexanoyl]amino]-4-oxobutanoyl]amino]-4-methylpentanoyl]amino]-3-(1H-indol-3-yl)propanoyl]amino]propanoyl]amino]propanoyl]amino]-5-oxopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]acetyl]amino]-5-carbamimidamidopentanoyl]amino]-4-carboxybutanoyl]amino]-4-methylpentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-4-methylsulfanylbutanoyl]amino]-3-hydroxypropanoyl]amino]-3-carboxypropanoyl]amino]-4-carboxybutanoyl]amino]-3-phenylpropanoyl]amino]-4-carboxybutanoyl]amino]acetyl]amino]-3-hydroxypropanoyl]amino]-3-phenylpropanoyl]amino]hexanoyl]amino]acetyl]amino]-4-methylpentanoic acid

Synonyms

Decanoyl-Lys-Asn-Leu-Trp-Ala-Ala-Gln-Arg-Tyr-Gly-Arg-Glu-Leu-Arg-Arg-Met-Ser-Asp-Glu-Phe-Glu-Gly-Ser-Phe-Lys-Gly-Leu-OH; N-decanoyl-L-lysyl-L-asparagyl-L-leucyl-L-tryptophyl-L-alanyl-L-alanyl-L-glutaminyl-L-arginyl-L-tyrosyl-glycyl-L-arginyl-L-alpha-glutamyl-L-leucyl-L-arginyl-L-arginyl-L-methionyl-L-seryl-L-alpha-aspartyl-L-alpha-glutamyl-L-phenylalanyl-L-alpha-glutamyl-glycyl-L-seryl-L-phenylalanyl-L-lysyl-glycyl-L-leucine

Appearance

Off-white Solid

Purity

≥95% by HPLC

Sequence

Decanoyl-KNLWAAQRYGRELRRMSDEFEGSFKGL

Storage

Store at -20°C

Solubility

Soluble in DMSO (10 mg/mL)

InChI

InChI=1S/C153H240N44O42S/c1-11-12-13-14-15-16-23-46-118(203)176-95(41-27-29-61-155)132(221)195-111(74-117(157)202)145(234)190-106(68-83(4)5)142(231)194-110(73-90-76-170-93-39-25-24-38-92(90)93)140(229)175-85(8)126(215)174-86(9)127(216)180-101(51-55-116(156)201)136(225)183-99(45-33-65-169-153(164)165)135(224)191-107(72-89-47-49-91(200)50-48-89)130(219)173-77-119(204)177-96(42-30-62-166-150(158)159)131(220)186-102(53-57-123(209)210)137(226)189-105(67-82(2)3)141(230)184-98(44-32-64-168-152(162)163)133(222)182-97(43-31-63-167-151(160)161)134(223)188-104(59-66-240-10)139(228)197-115(81-199)148(237)196-112(75-125(213)214)146(235)187-103(54-58-124(211)212)138(227)192-108(70-87-34-19-17-20-35-87)144(233)185-100(52-56-122(207)208)129(218)172-79-121(206)179-114(80-198)147(236)193-109(71-88-36-21-18-22-37-88)143(232)181-94(40-26-28-60-154)128(217)171-78-120(205)178-113(149(238)239)69-84(6)7/h17-22,24-25,34-39,47-50,76,82-86,94-115,170,198-200H,11-16,23,26-33,40-46,51-75,77-81,154-155H2,1-10H3,(H2,156,201)(H2,157,202)(H,171,217)(H,172,218)(H,173,219)(H,174,215)(H,175,229)(H,176,203)(H,177,204)(H,178,205)(H,179,206)(H,180,216)(H,181,232)(H,182,222)(H,183,225)(H,184,230)(H,185,233)(H,186,220)(H,187,235)(H,188,223)(H,189,226)(H,190,234)(H,191,224)(H,192,227)(H,193,236)(H,194,231)(H,195,221)(H,196,237)(H,197,228)(H,207,208)(H,209,210)(H,211,212)(H,213,214)(H,238,239)(H4,158,159,166)(H4,160,161,167)(H4,162,163,168)(H4,164,165,169)/t85-,86-,94-,95-,96-,97-,98-,99-,100-,101-,102-,103-,104-,105-,106-,107-,108-,109-,110-,111-,112-,113-,114-,115-/m0/s1

InChI Key

GVCUYYAHIMOGMN-BAOXYPIUSA-N

Canonical SMILES

CCCCCCCCCC(=O)NC(CCCCN)C(=O)NC(CC(=O)N)C(=O)NC(CC(C)C)C(=O)NC(CC1=CNC2=CC=CC=C21)C(=O)NC(C)C(=O)NC(C)C(=O)NC(CCC(=O)N)C(=O)NC(CCCNC(=N)N)C(=O)NC(CC3=CC=C(C=C3)O)C(=O)NCC(=O)NC(CCCNC(=N)N)C(=O)NC(CCC(=O)O)C(=O)NC(CC(C)C)C(=O)NC(CCCNC(=N)N)C(=O)NC(CCCNC(=N)N)C(=O)NC(CCSC)C(=O)NC(CO)C(=O)NC(CC(=O)O)C(=O)NC(CCC(=O)O)C(=O)NC(CC4=CC=CC=C4)C(=O)NC(CCC(=O)O)C(=O)NCC(=O)NC(CO)C(=O)NC(CC5=CC=CC=C5)C(=O)NC(CCCCN)C(=O)NCC(=O)NC(CC(C)C)C(=O)O

1. Role of Bcl-2 family proteins in apoptosis: apoptosomes or mitochondria?

Y Tsujimoto Genes Cells. 1998 Nov;3(11):697-707. doi: 10.1046/j.1365-2443.1998.00223.x.

Apoptosis is an essential physiological process for the selective elimination of cells, which is involved in a variety of biological events. The Bcl-2 family is the best characterized protein family involved in the regulation of apoptotic cell death, consisting of anti-apoptotic and pro-apoptotic members. The anti-apoptotic members of this family, such as Bcl-2 and Bcl-XL, prevent apoptosis either by sequestering proforms of death-driving cysteine proteases called caspases (a complex called the apoptosome) or by preventing the release of mitochondrial apoptogenic factors such as cytochrome c and AIF (apoptosis-inducing factor) into the cytoplasm. After entering the cytoplasm, cytochrome c and AIF directly activate caspases that cleave a set of cellular proteins to cause apoptotic changes. In contrast, pro-apoptotic members of this family, such as Bax and Bak, trigger the release of caspases from death antagonists via heterodimerization and also by inducing the release of mitochondrial apoptogenic factors into the cytoplasm via acting on mitochondrial permeability transition pore, thereby leading to caspase activation. Thus, the Bcl-2 family of proteins acts as a critical life-death decision point within the common pathway of apoptosis.

2. BCL-2 family proteins: changing partners in the dance towards death

Justin Kale, Elizabeth J Osterlund, David W Andrews Cell Death Differ. 2018 Jan;25(1):65-80. doi: 10.1038/cdd.2017.186. Epub 2017 Nov 17.

The BCL-2 family of proteins controls cell death primarily by direct binding interactions that regulate mitochondrial outer membrane permeabilization (MOMP) leading to the irreversible release of intermembrane space proteins, subsequent caspase activation and apoptosis. The affinities and relative abundance of the BCL-2 family proteins dictate the predominate interactions between anti-apoptotic and pro-apoptotic BCL-2 family proteins that regulate MOMP. We highlight the core mechanisms of BCL-2 family regulation of MOMP with an emphasis on how the interactions between the BCL-2 family proteins govern cell fate. We address the critical importance of both the concentration and affinities of BCL-2 family proteins and show how differences in either can greatly change the outcome. Further, we explain the importance of using full-length BCL-2 family proteins (versus truncated versions or peptides) to parse out the core mechanisms of MOMP regulation by the BCL-2 family. Finally, we discuss how post-translational modifications and differing intracellular localizations alter the mechanisms of apoptosis regulation by BCL-2 family proteins. Successful therapeutic intervention of MOMP regulation in human disease requires an understanding of the factors that mediate the major binding interactions between BCL-2 family proteins in cells.

3. The application of nanoparticles in cancer immunotherapy: Targeting tumor microenvironment

Muyue Yang, Jipeng Li, Ping Gu, Xianqun Fan Bioact Mater. 2020 Dec 26;6(7):1973-1987. doi: 10.1016/j.bioactmat.2020.12.010. eCollection 2021 Jul.

The tumor development and metastasis are closely related to the structure and function of the tumor microenvironment (TME). Recently, TME modulation strategies have attracted much attention in cancer immunotherapy. Despite the preliminary success of immunotherapeutic agents, their therapeutic effects have been restricted by the limited retention time of drugs in TME. Compared with traditional delivery systems, nanoparticles with unique physical properties and elaborate design can efficiently penetrate TME and specifically deliver to the major components in TME. In this review, we briefly introduce the substitutes of TME including dendritic cells, macrophages, fibroblasts, tumor vasculature, tumor-draining lymph nodes and hypoxic state, then review various nanoparticles targeting these components and their applications in tumor therapy. In addition, nanoparticles could be combined with other therapies, including chemotherapy, radiotherapy, and photodynamic therapy, however, the nanoplatform delivery system may not be effective in all types of tumors due to the heterogeneity of different tumors and individuals. The changes of TME at various stages during tumor development are required to be further elucidated so that more individualized nanoplatforms could be designed.