956479-18-8
Chemical Structure
GB111-NH2
- CAS No.: 956479-18-8
- Formula:C33H39N3O6
- Molecular Weight:573.68
IUPAC Name: (S)-7-amino-3-((S)-2-(((benzyloxy)carbonyl)amino)-3-phenylpropanamido)-2-oxoheptyl 2,6-dimethylbenzoate
InChIKey: SRXNAWHDCFMFNI-NSOVKSMOSA-N
SMILES: O=C(OCC([C@@H](NC([C@@H](NC(OCC1=CC=CC=C1)=O)CC2=CC=CC=C2)=O)CCCCN)=O)C3=C(C)C=CC=C3C
Biological Activity: GB111-NH2 is a covalent cysteine cathepsin inhibitor. GB111-NH2 blocks cathepsin B/L/S activity, probe binding, and BMV109 signal in biopsy tissue. GB111-NH2 blocks brain cathepsin GB123 binding under ex vivo conditions. GB111-NH2 induces oxidative stress, autophagy inhibition, apoptosis, proliferation/S-phase entry, arginase activity, and non-autonomous apoptosis of neighboring tumor cells. GB111-NH2 reduces primary breast tumor volume, causes tumor regression, and alters macrophage morphology. GB111-NH2 restores marginal zone architecture and elevates lymphotoxin α (LTα) and splenic lymphotoxin β receptor (LTβR) signaling. GB111-NH2 can be used for research on chronic epilepsy, breast cancer, and atherosclerosis[1][2][3][4][5][6].
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GB111-NH2 | GB111-NH2 is a covalent cysteine cathepsin inhibitor. GB111-NH2 blocks cathepsin B/L/S activity, probe binding, and BMV109 signal in biopsy tissue. GB111-NH2 blocks brain cathepsin GB123 binding under ex vivo conditions. GB111-NH2 induces oxidative stress, autophagy inhibition, apoptosis, proliferation/S-phase entry, arginase activity, and non-autonomous apoptosis of neighboring tumor cells. GB111-NH2 reduces primary breast tumor volume, causes tumor regression, and alters macrophage morphology. GB111-NH2 restores marginal zone architecture and elevates lymphotoxin α (LTα) and splenic lymphotoxin β receptor (LTβR) signaling. GB111-NH2 can be used for research on chronic epilepsy, breast cancer, and atherosclerosis. | |||||||||||||||||||||
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References
- [1]. Tsvirkun D, et al. CT Imaging of Enzymatic Activity in Cancer Using Covalent Probes Reveal a Size-Dependent Pattern. Journal of the American Chemical Society. 2018 Sep 26;140(38):12010-12020.
- [2]. Hamed R, et al. Challenges in Batch-to-Bed Translation Involving Inflammation-Targeting Compounds in Chronic Epilepsy: The Case of Cathepsin Activity-Based Probes. ACS omega. 2024 Feb 13;9(6):6965-6975.
- [3]. Withana NP, et al. Labeling of active proteases in fresh-frozen tissues by topical application of quenched activity-based probes. Nature protocols. 2016 Jan;11(1):184-91.
- [4]. Salpeter SJ, et al. A novel cysteine cathepsin inhibitor yields macrophage cell death and mammary tumor regression. Oncogene. 2015 Dec 10;34(50):6066-78. [Content Brief]
- [5]. Meena NK, et al. mTORC1 activation in B cells confers impairment of marginal zone microarchitecture by exaggerating cathepsin activity. Immunology. 2018 Dec;155(4):505-518.
- [6]. Abu-Fanne R, et al. α-Defensins Induce a Post-translational Modification of Low Density Lipoprotein (LDL) That Promotes Atherosclerosis at Normal Levels of Plasma Cholesterol. The Journal of biological chemistry. 2016 Feb 05;291(6):2777-86.
