The power of sulfhydryl groups: Thiolated lipid-based nanoparticles enhance cellular uptake of nucleic acids.

Aim: The aim of the study was to evaluate the effect of thiolation of lipid-based nanoparticles (LNPs) on cellular uptake of nucleic acids.

Methods: A thiolated surfactant was synthesized by binding palmitic acid covalently to cysteine. Green fluorescent protein (GFP) encoding plasmid DNA (pDNA) was used as model nucleic acid and incorporated via hydrophobic ion-pairing with a cationic cholesterol derivate (DcCholesterol) in LNPs that were prepared by solvent injection method using the thiolated surfactant for surface decoration.

Development of Cytotoxic GW7604-Zeise's Salt Conjugates as Multitarget Compounds with Selectivity for Estrogen Receptor- Positive Tumor Cells.

()-3-(4-(()-1-(4-Hydroxyphenyl)-2-phenylbut-1-enyl)phenyl)acrylic acid () as a carrier was esterified with alkenols of various lengths and coordinated through the ethylene moiety to PtCl, similar to Zeise's salt (K[PtCl(CH)]). The resulting complexes (Alk = Prop, But, Pent, Hex) degraded in aqueous solution only by exchange of the chlorido ligands. For example, coordinated the amino acid alanine in the cell culture medium, bound the isolated nucleotide 5'-GMP, and interacted with the DNA (empty plasmid pSport1).

Reaction Behavior of [1,3-Diethyl-4,5-diphenyl-1-imidazol-2-ylidene] Containing Gold(I/III) Complexes against Ingredients of the Cell Culture Medium and the Meaning on the Potential Use for Cancer Eradication Therapy.

The reactivities of halido[1,3-diethyl-4,5-diphenyl-1-imidazol-2-ylidene]gold(I) (chlorido (), bromido (), iodido ()), bis[1,3-diethyl-4,5-diphenyl-1-imidazol-2-ylidene]gold(I) (), and bis[1,3-diethyl-4,5-diphenyl-1-imidazol-2-ylidene]dihalidogold(III) (chlorido (), bromido (), iodido ()) complexes against ingredients of the cell culture medium were analyzed by HPLC. The degradation in the RPMI 1640 medium was studied, too. Complex quantitatively reacted with chloride to , while showed additionally ligand scrambling to .

Development of heterodimeric estrogen receptor alpha antagonists to target simultaneously the ligand and coactivator binding site.

One-third of breast cancer patients will develop recurrent cancer within 15 years of endocrine treatment. Notably, tumor growth in a hormone-refractory state still relies on the interaction between estrogen receptor alpha (ERα) and upregulated coactivators. Herein, we suggest that simultaneous targeting of the primary ligand binding site (LBS) and the coactivator binding site (CABS) at ERα represents a promising alternative therapeutic strategy to overcome mutation-driven resistance in breast cancer.

Investigations of the reactivity, stability and biological activity of halido (NHC)gold(I) complexes.

The significance of the halido ligand (Cl, Br, I) in halido[3-ethyl-4-phenyl-5-(2-methoxypyridin-5-yl)-1-propyl-1,3-dihydro-2-imidazol-2-ylidene]gold(I) complexes (2-4) in terms of ligand exchange reactions, including the ligand scrambling to the bis[3-ethyl-4-phenyl-5-(2-methoxypyridin-5-yl)-1-propyl-1,3-dihydro-2-imidazol-2-ylidene]gold(I) complex (5), was evaluated by HPLC in acetonitrile/water = 50:50 (v/v) mixtures. In the presence of 0.9% NaCl, the bromido (NHC)gold(I) complex 3 was immediately transformed into the chlorido (NHC)gold(I) complex 2.