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Clindamycin 2-phosphate_Molecular_structure_CAS_24729-96-2)
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Clindamycin 2-phosphate

Catalog No. C6427 Name Sigma Aldrich
CAS Number 24729-96-2 Website http://www.sigmaaldrich.com
M. F. C18H34ClN2O8PS Telephone 1-800-521-8956
M. W. 504.962921 Fax
Purity Email
Storage Chembase ID: 132629

SYNONYMS

IUPAC name
{[(2R,3R,4S,5R)-6-[(2S)-2-chloro-1-{[(2S,4R)-1-methyl-4-propylpyrrolidin-2-yl]formamido}propyl]-4,5-dihydroxy-2-(methylsulfanyl)oxan-3-yl]oxy}phosphonic acid
IUPAC Traditional name
[(2R,3R,4S,5R)-6-[(2S)-2-chloro-1-{[(2S,4R)-1-methyl-4-propylpyrrolidin-2-yl]formamido}propyl]-4,5-dihydroxy-2-(methylsulfanyl)oxan-3-yl]oxyphosphonic acid
Synonyms
Clindamycin 2-dihydrogen phosphate

DATABASE IDS

PubChem SID 24892866
MDL Number MFCD07793328
CAS Number 24729-96-2
EC Number 246-433-0

PROPERTIES

GHS Pictograms GHS07
GHS Signal Word Warning
GHS Hazard statements H302
European Hazard Symbols Harmful Harmful (Xn)
Personal Protective Equipment dust mask type N95 (US), Eyeshields, Gloves
Risk Statements 22
RTECS GF2625000
Safety Statements 36
Storage Temperature 2-8°C
German water hazard class 3

DETAILS

Description (English)
Biochem/physiol Actions
Spectrum of Activity: Gram positive cocci and taxoplasma. Especially active against anaerobic bacteria.Mode of Action: Inhibits protein synthesis in bacterial by binding the 50s ribosomal subunit.
Clindamycin 2-phosphate is a pharmacological tyrosyl-DNA phosphodiesterase (Tdp1) inhibitor. Clindamycin 2-phosphate can repair DNA topoisomerase I-DNA covalent complexes by hydrolyzing the tyrosyl-DNA bond. It inhibits protein synthesis in bacteria by binding the 50s ribosomal subunit. 2. Spectrum of Activity: Gram positive cocci and taxoplasma. Especially active against anaerobic bacteria.
Other Notes
Antibacterial and antiprotozoal antibiotic of the licosamide class.
Application
Clindamycin 2-phosphate is an aminoglycoside antibiotic that has been used to study the cytoxicity of antibiotics on human cell lines 1, Bacterial protein synthesis and peptide translation, and the inhibition of human Tyrosyl-DNA Phosphodiesterase 2.

REFERENCES