Aspartic acid tagged carbon nanotubols as a tool to deliver docetaxel to breast cancer cells: Reduced hemotoxicity with improved cytotoxicity.

08:00 EDT 12th April 2019 | BioPortfolio

Summary of "Aspartic acid tagged carbon nanotubols as a tool to deliver docetaxel to breast cancer cells: Reduced hemotoxicity with improved cytotoxicity."

The present study aimed to explore the potential of hydroxylated carbon nanotubes (CNTnols) conjugated with aspartic acid for the delivery of docetaxel (DTX) to breast cancer cells. The conjugate was well-characterized by FT-IR, NMR, XRD and FE-SEM. The nanoconjugate offered a hydrodynamic diameter of 86.31 ± 1.02 nm, with a PDI of 0.113 and zeta potential of -41.6 ± 0.17 mV. The designed nanosystem offered a controlled & pH dependent release vouching release of drug in the cancerous cytosol, not in blood, assuring delivery of the pay-load to the site of action. The carriers offered substantial hemocompatibility and lower plasma protein binding, insuring more drug available for the site of action. The in-vitro cell viability studies in MDA MB-231 cells inferred approx. 2.8 times enhancement in the cytotoxicity potential of the conjugate vis-à-vis plain drug. Pharmacokinetic studies also corroborated the superiority of the designed nanoconjugate intern of enhanced bioavailable fractions, reduced clearance and longer residence to that of plain docetaxel. The present studies, successfully provide a workable nanomedicine loaded with a BCS class-IV drug for improved efficacy and safety in breast cancer.


Journal Details

This article was published in the following journal.

Name: Toxicology in vitro : an international journal published in association with BIBRA
ISSN: 1879-3177


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Medical and Biotech [MESH] Definitions

A subclass of peptide hydrolases that depend on an ASPARTIC ACID residue for their activity.

The D-isomer of ASPARTIC ACID.

A sub-subclass of endopeptidases that depend on an ASPARTIC ACID residue for their activity.

An ASPARTIC ACID residue in polypeptide chains that is linked at the beta-carboxyl group instead of at the normal, alpha-carboxyl group, polypeptide linkage. It is a result of the spontaneous decomposition of aspartic acid or ASPARAGINE residues.

An enzyme that catalyzes the formation of beta-aspartyl phosphate from aspartic acid and ATP. Threonine serves as an allosteric regulator of this enzyme to control the biosynthetic pathway from aspartic acid to threonine. EC

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