Structural Characterization of Cis- and Trans-Pt(NH)Cl Conjugations with Chitosan Nanoparticles.

The conjugation of chitosan 15 and 100 KD with anticancer drugs cis- and trans-Pt (NH)Cl (abbreviated cis-Pt and trans-Pt) were studied at pH 5-6. Using multiple spectroscopic methods and thermodynamic analysis to characterize the nature of drug-chitosan interactions and the potential application of chitosan nanoparticles in drug delivery. Analysis showed that both hydrophobic and hydrophilic contacts are involved in drug-polymer interactions, while chitosan size and charge play a major role in the stability of drug-polymer complexes.

DNA acidification by citric acid and gallic acid: acid binding site and DNA structural dynamics.

Communicated by Ramaswamy H. Sarma.

Locating the binding sites of two aminobenzoic acid derivatives on tRNA: drug binding efficacy and RNA structure.

The binding of tRNA to aminobenzoic acid derivatives DAB-0 (-[4-(2,5-dioxo-pyrrolidin-1-yl)-benzoyl]-hydrazine carboxylic acid -butyl ester) and DAB-1 (-[4-(2,5-dioxo-2,5-dihydro-pyrrol-1-yl)-benzoyl]-hydrazine carboxylic acid -butyl ester) was investigated in aqueous solution at physiological pH. Thermodynamic parameters Δ -4.8 to -4.

Locating the binding sites of citric acid and gallic acid on milk -lactoglobulin.

-Lactoglobulin (-LG) is a member of lipocalin superfamily of transporters for small hydrophobic and hydrophilic molecules. We located the binding sites of citric acid and gallic acid on -lactoglobulin (-LG) in aqueous solution at physiological conditions, using spectroscopic methods, thermodynamic analysis and molecular modeling. Thermodynamic parameters Δ -9.

Binding efficacy of aminobenzoic acid derivatives with DNA duplex: drug binding sites and DNA structure and dynamics.

Communicated by Ramaswamy H. Sarma.

Biomolecular study and conjugation of two para-aminobenzoic acid derivatives with serum proteins: drug binding efficacy and protein structural analysis.

Two aminobenzoic acid derivatives DAB-0 and DAB-1 showed distinct biological properties on murine bladder cancer (BCa) cell line MB49-I. In contrast to DAB-1, DAB-0 does not possess any anti-inflammatory activity and is less toxic. Furthermore, DAB-0 does not interfere with INFγ-induced STAT1 activation and TNFα-induced IκB phosphorylation, while DAB-1 does.

Application and biomolecular study of functionalized folic acid-dendrimer nanoparticles in drug delivery.

We determined the loading efficacy of folic acid PAMAM G3 and folic acid PAMAM G4 nanoparticles with doxorubicin (Dox), tamoxifen (Tam) and tetracycline (Tet) in aqueous solution at pH 7.2. Thermodynamic parameters Δ -16 to -4 (kJ mol), Δ 31 to -0.

Complexation of cis-Pt and trans-Pt(NH)Cl with serum proteins: A potential application for drug delivery.

AbbreviationsHAShuman serum albuminBSAbovine serum albumin-LGbeta-lactoglobulincis-Pt and trans-PtPt(NH)ClFTIRFourier transform infraredCommunicated by Ramaswamy H. Sarma.

Conjugation of vitamin C with serum proteins: A potential application for vitamin delivery.

Vitamin C plays an important role in human health and therefore, the bioavailability and delivery of this micronutrient in solution have been the subject of intensive studies. Serum proteins are known to play an important role as drug delivery tools with important clinical applications. The conjugation of l-ascorbic acid with human serum albumin (HSA), bovine serum albumin (BSA) and beta-lactoglobulin (β-LG) was investigated in aqueous solution at physiological pH.

Effect of tea catechins on tRNA structure and dynamics.

AbbreviationsCcatechinECGepicatechin gallateEGCGEpigallocatechin gallateAAdenineCcytosineGGuanineUuracilFTIRFourier transform infraredCommunicated by Ramaswamy H. Sarma.

Structural dynamics of DNA binding to tea catechins.

We determined the conjugation and binding efficacy of tea catechins (+)-catechin (C), (-)-epicatechin gallate (ECG) and (-)-epigallocatechin gallate (EGCG) with calf thymus DNA in aqueous solution at physiological pH. Thermodynamic analysis showed that tea catechins bind DNA via hydrophilic and hydrophobic interactions with the binding efficacy of 45-60%. Larger catechins form more stable DNA adducts with the order of stability EGCG > ECG > C.

Location of multiple binding sites for testo and testo-Pt(II) with tRNA.

We report the binding of testo and testo-Pt(II) complexes (testosterone derivatives) with tRNA in aqueous solution at physiological pH. Thermodynamic parameter Δ -8 to -3 (kJ mol), Δ 35 to 18 (J molK) and Δ -14 to -13 (kJ mol) and other spectroscopic results showed drug-tRNA binding occurs via ionic contacts with testo-Pt(II) forming more stable tRNA complexes in comparison to testo: -Pt(II)-tRNA= 3.2 (± 0.

Testo and testo-Pt(II) bind DNA at different locations.

The development of new targeted anticancer agents able to efficiently and specifically destroy cancer cells with minimal toxic side effects is nowadays a subject of intensive research endeavors. We report the conjugation of testo and testo-Pt(II) (two semi-synthetic testosterone derivatives) with calf thymus DNA in aqueous solution at physiological pH. Multiple spectroscopic methods, thermodynamic analysis and modeling were used to determine the binding efficacy of these drugs to DNA duplex.

Conjugation of testo and testo-Pt(II) with serum proteins: Loading efficacy and protein conformation.

The potential application of hybrid anticancer molecules requires further investigation. There is a great interest in developing new site-specific anticancer agents able to efficiently destroy cancer cells with minimal toxic side effects. Serum proteins are known to play an important role as drug delivery system with important clinical applications.

An Overview of the Loading Efficacy of Cationic Lipids with Milk Proteins: A Potential Application for Lipid Delivery.

In this review, the loading efficacies of helper and Cationic Lipids Cholesterol (CHOL), 1,2-dioleoyl-3-trimethylammonium-propane (DOTAP), Dioctadecyl Dimethyl- Ammonium Bromide (DDAB) and Dioleoyl Phosphatidylethanolamine (DOPE) with milk β- lactoglobulin, α-casein and β-casein were compared in aqueous solution at physiological conditions. Structural analysis showed that lipids bind milk proteins via hydrophilic, hydrophobic and H-bonding contacts with DOTAP and DDAB forming more stable protein conjugates. Loading efficacy was 30-50% and enhanced with cationic lipids.

DNA binding efficacy with functionalized folic acid-PAMAM nanoparticles.

Functionalized folic-polymers were often used for gene and drug delivery. DNA binding to folic acid-PAMAM conjugates was studied, using multiple spectroscopic methods, thermodynamic analysis and transmission electron microscopy (TEM). Thermodynamic parameters showed DNA-folic acid-PAMAM conjugation occurs via H-bonding, hydrophobic and van der Waals contacts.

Encapsulation of micronutrients resveratrol, genistein, and curcumin by folic acid-PAMAM nanoparticles.

It has been shown that encapsulation of dietary polyphenols leads to increased solubility and bioavailability of these micronutrients. The encapsulation of dietary polyphenols resveratrol, genistein, and curcumin by folic acid-PAMAM-G3 and folic acid-PAMAM-G4 nanoparticles was studied in aqueous solution at physiological conditions, using multiple spectroscopic methods, TEM images, and docking studies. The polyphenol bindings are via hydrophilic, hydrophobic, and H-bonding contacts with resveratrol forming more stable conjugates.

Binding efficacy of tRNA with folic acid-PAMAM nanoparticles.

tRNA binding efficacy to folic acid-PAMAM nanoparticles was determined, using multiple spectroscopic methods, thermodynamic analysis and transmission electron microscopy (TEM). The structural analysis showed tRNA binds folic acid-PAMAM through H-bonding, hydrophobic and van der Waals contacts. As PAMAM size increases the binding efficacy and the stability of tRNA conjugates are enhanced.

Binding analysis of antioxidant polyphenols with PAMAM nanoparticles.

Dietary polyphenols are abundant micronutrients in our diet and paly major role in prevention of degenerative diseases. The binding efficacy of antioxidant polyphenols resveratrol, genistein, and curcumin with PAMAM-G3 and PAMAM-G4 nanoparticles was investigated in aqueous solution at physiological conditions, using multiple spectroscopic methods, TEM images, and docking studies. The polyphenol bindings are via hydrophilic, hydrophobic, and H-bonding contacts with resveratrol forming more stable conjugates.

tRNA conjugation with folic acid-chitosan conjugates.

The conjugation of tRNA with folic acid-chitosan conjugates was studied, using multiple spectroscopic methods and transmission electron microscopy (TEM). Thermodynamic analysis ΔH -14 to -10 (KJMol) and ΔS 14 to -1 (JMol, K) showed tRNA-folic acid-chitosan bindings occur via H-bonding, hydrophobic and van der Waals contacts. The loading efficacy and the stability of tRNA conjugates were enhanced as folic acid-chitosan size increased.

Characterization of folic acid-PAMAM conjugates: drug loading efficacy and dendrimer morphology.

We report the loading efficacy of folic acid (FA) by polyamidoamine (PAMAM-G3 and PAMAM-G4) nanoparticles in aqueous solution at physiological pH. Thermodynamic parameters ΔH = -47.57 (kJ Mol), ΔS = -122.

Al cation induces aggregation of serum proteins.

Al cation is known to induce protein fibrillation and causes several neurodegenerative disorders. We report the spectroscopic, thermodynamic analysis and AFM imaging for the Al cation binding process with human serum albumin (HSA), bovine serum albumin (BSA) and milk beta-lactoglobulin (b-LG) in aqueous solution at physiological pH. Hydrophobicity played a major role in Al-protein interactions with more hydrophobic b-LG forming stronger Al-protein complexes.

Aggregation of trypsin and trypsin inhibitor by Al cation.

Al cation may trigger protein structural changes such as aggregation and fibrillation, causing neurodegenerative diseases. We report the effect of Al cation on the solution structures of trypsin (try) and trypsin inhibitor (tryi), using thermodynamic analysis, UV-Visible, Fourier transform infrared (FTIR) spectroscopic methods and atomic force microscopy (AFM). Thermodynamic parameters showed Al-protein bindings occur via H-bonding and van der Waals contacts for trypsin and trypsin inhibitor.