BENDAMUSTINE

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Search structure


Trade Names	BENDAMUSTINE
Synonyms	Bendamustine
Status
Molecule Category	Free-form
ATC	L01AA09
UNII	9266D9P3PQ
EPA CompTox	DTXSID2046888


Active Pharmaceutical Ingredients Bioactive chemicals	Exact Similarity SubStructure	Threshold (%) >= 70

Structure


InChI Key	YTKUWDBFDASYHO-UHFFFAOYSA-N
Smiles	Cn1c(CCCC(=O)O)nc2cc(N(CCCl)CCCl)ccc21
InChI	InChI=1S/C16H21Cl2N3O2/c1-20-14-6-5-12(21(9-7-17)10-8-18)11-13(14)19-15(20)3-2-4-16(22)23/h5-6,11H,2-4,7-10H2,1H3,(H,22,23)

Physicochemical Descriptors

Property Name	Value
Molecular Formula	C16H21Cl2N3O2
Molecular Weight	358.27
AlogP	3.26
Hydrogen Bond Acceptor	4.0
Hydrogen Bond Donor	1.0
Number of Rotational Bond	9.0
Polar Surface Area	58.36
Molecular species	ACID
Aromatic Rings	2.0
Heavy Atoms	23.0

Assay Description	Organism	Bioactivity	Reference
Inhibition of human OATP1B3-mediated [3H]CCK-8 at 100 uM after 5 mins relative to control	Homo sapiens	48.8 %
Enzymatic Assay: Hydroxamic acid is a well know metal-chelating agent, especially for Zn atom. The hydroxamic acid moiety has been demonstrated as the key structural element in many highly potent and selective inhibitors against a variety of metalloenzymes, such as matrix metalloproteinases (MMP), tumor necrosis factor-alpha converting enzyme (TACE), Histone Deacetylase (HDAC), Peptidyl deformylase (PDF), A Disintegrin And Metalloproteinase (ADAM), UDP-3-O[R-3-hydroxymyristoyl]-GlcNAc deacetylase, Clostridium Histolytium Collagenase (ChC), Procollagen C-Proteinase (PCP), and Aggrecanase. Many of these metalloenzymes are well known important disease target, such as HDAC and MMP. All hydroxamic acid compounds exemplified in the application have been tested against one or multiple metalloenzymes. The following protocol is used to assay the compounds of the invention against the HDAC enzymes.The buffer used in this assay is 25 mM HEPES, pH 8.0, 137 mM NaCl, 2.7 mM KCl, 1 mM MgCl2 and the substrate is Boc.	Homo sapiens	17.0 nM
Enzymatic Assay: Hydroxamic acid is a well know metal-chelating agent, especially for Zn atom. The hydroxamic acid moiety has been demonstrated as the key structural element in many highly potent and selective inhibitors against a variety of metalloenzymes, such as matrix metalloproteinases (MMP), tumor necrosis factor-alpha converting enzyme (TACE), Histone Deacetylase (HDAC), Peptidyl deformylase (PDF), A Disintegrin And Metalloproteinase (ADAM), UDP-3-O[R-3-hydroxymyristoyl]-GlcNAc deacetylase, Clostridium Histolytium Collagenase (ChC), Procollagen C-Proteinase (PCP), and Aggrecanase. Many of these metalloenzymes are well known important disease target, such as HDAC and MMP. All hydroxamic acid compounds exemplified in the application have been tested against one or multiple metalloenzymes. The following protocol is used to assay the compounds of the invention against the HDAC enzymes.The buffer used in this assay is 25 mM HEPES, pH 8.0, 137 mM NaCl, 2.7 mM KCl, 1 mM MgCl2 and the substrate is Boc.	Homo sapiens	9.0 nM
Enzymatic Assay: Hydroxamic acid is a well know metal-chelating agent, especially for Zn atom. The hydroxamic acid moiety has been demonstrated as the key structural element in many highly potent and selective inhibitors against a variety of metalloenzymes, such as matrix metalloproteinases (MMP), tumor necrosis factor-alpha converting enzyme (TACE), Histone Deacetylase (HDAC), Peptidyl deformylase (PDF), A Disintegrin And Metalloproteinase (ADAM), UDP-3-O[R-3-hydroxymyristoyl]-GlcNAc deacetylase, Clostridium Histolytium Collagenase (ChC), Procollagen C-Proteinase (PCP), and Aggrecanase. Many of these metalloenzymes are well known important disease target, such as HDAC and MMP. All hydroxamic acid compounds exemplified in the application have been tested against one or multiple metalloenzymes. The following protocol is used to assay the compounds of the invention against the HDAC enzymes.The buffer used in this assay is 25 mM HEPES, pH 8.0, 137 mM NaCl, 2.7 mM KCl, 1 mM MgCl2 and the substrate is Boc.	Homo sapiens	6.0 nM
Enzymatic Assay: Hydroxamic acid is a well know metal-chelating agent, especially for Zn atom. The hydroxamic acid moiety has been demonstrated as the key structural element in many highly potent and selective inhibitors against a variety of metalloenzymes, such as matrix metalloproteinases (MMP), tumor necrosis factor-alpha converting enzyme (TACE), Histone Deacetylase (HDAC), Peptidyl deformylase (PDF), A Disintegrin And Metalloproteinase (ADAM), UDP-3-O[R-3-hydroxymyristoyl]-GlcNAc deacetylase, Clostridium Histolytium Collagenase (ChC), Procollagen C-Proteinase (PCP), and Aggrecanase. Many of these metalloenzymes are well known important disease target, such as HDAC and MMP. All hydroxamic acid compounds exemplified in the application have been tested against one or multiple metalloenzymes. The following protocol is used to assay the compounds of the invention against the HDAC enzymes.The buffer used in this assay is 25 mM HEPES, pH 8.0, 137 mM NaCl, 2.7 mM KCl, 1 mM MgCl2 and the substrate is Boc.	Homo sapiens	72.0 nM
Enzymatic Assay: Hydroxamic acid is a well know metal-chelating agent, especially for Zn atom. The hydroxamic acid moiety has been demonstrated as the key structural element in many highly potent and selective inhibitors against a variety of metalloenzymes, such as matrix metalloproteinases (MMP), tumor necrosis factor-alpha converting enzyme (TACE), Histone Deacetylase (HDAC), Peptidyl deformylase (PDF), A Disintegrin And Metalloproteinase (ADAM), UDP-3-O[R-3-hydroxymyristoyl]-GlcNAc deacetylase, Clostridium Histolytium Collagenase (ChC), Procollagen C-Proteinase (PCP), and Aggrecanase. Many of these metalloenzymes are well known important disease target, such as HDAC and MMP. All hydroxamic acid compounds exemplified in the application have been tested against one or multiple metalloenzymes. The following protocol is used to assay the compounds of the invention against the HDAC enzymes.The buffer used in this assay is 25 mM HEPES, pH 8.0, 137 mM NaCl, 2.7 mM KCl, 1 mM MgCl2 and the substrate is Boc.	Homo sapiens	25.0 nM
Enzymatic Assay: Hydroxamic acid is a well know metal-chelating agent, especially for Zn atom. The hydroxamic acid moiety has been demonstrated as the key structural element in many highly potent and selective inhibitors against a variety of metalloenzymes, such as matrix metalloproteinases (MMP), tumor necrosis factor-alpha converting enzyme (TACE), Histone Deacetylase (HDAC), Peptidyl deformylase (PDF), A Disintegrin And Metalloproteinase (ADAM), UDP-3-O[R-3-hydroxymyristoyl]-GlcNAc deacetylase, Clostridium Histolytium Collagenase (ChC), Procollagen C-Proteinase (PCP), and Aggrecanase. Many of these metalloenzymes are well known important disease target, such as HDAC and MMP. All hydroxamic acid compounds exemplified in the application have been tested against one or multiple metalloenzymes. The following protocol is used to assay the compounds of the invention against the HDAC enzymes.The buffer used in this assay is 25 mM HEPES, pH 8.0, 137 mM NaCl, 2.7 mM KCl, 1 mM MgCl2 and the substrate is Boc.	Homo sapiens	107.0 nM
SARS-CoV-2 3CL-Pro protease inhibition percentage at 20µM by FRET kind of response from peptide substrate	Severe acute respiratory syndrome coronavirus 2	78.33 %
Antiviral activity determined as inhibition of SARS-CoV-2 induced cytotoxicity of VERO-6 cells at 10 uM after 48 hours exposure to 0.01 MOI SARS CoV-2 virus by high content imaging	Chlorocebus sabaeus	-0.1 %		Antiviral activity determined as inhibition of SARS-CoV-2 induced cytotoxicity of VERO-6 cells at 10 uM after 48 hours exposure to 0.01 MOI SARS CoV-2 virus by high content imaging	Chlorocebus sabaeus	-0.1 %

Related Entries

Cross References

Resources	Reference
ChEBI	135515
ChEMBL	CHEMBL487253
DrugBank	DB06769
DrugCentral	302
FDA SRS	9266D9P3PQ
Guide to Pharmacology	7478
PubChem	65628
SureChEMBL	SCHEMBL26319
ZINC	ZINC000004214955

CONTENTS

PREMIER has received funding from the Innovative Medicines Initiative 2 Joint Undertaking (JU) under grant agreement No 875508. The JU receives support from the EU’s Horizon 2020 research and innovation programme and the European Federation of Pharmaceutical Industries and Associations (EFPIA). The views reflect only the authors’ perspective and the JU is not responsible for any use that may be made of the information this manuscript contains.

Elements of the website have been developed under projects PREMIER and the Biocenter Finland Drug Discovery and Chemical Biology network. CSC-IT is thanked for providing computational resources. Content of the website is provided without guarantee for correctness. Data has been collected and integrated from multiple public sources, for the largest: FDA, HUGO Gene Nomenclature Committee, ChEMBL, IUPHAR/BPS guide to pharmacology, Reactome, UniProt, and Ensembl. Credit is given to Ensembl for collecting species images (provided under public domain licences such as Wikimedia and NHGRI).