Syntheses and Preliminary Study on the DNA-Binding Property of Nicotinoyl Aspartic Acid Dipeptide and Tetrapeptide
نویسنده
چکیده
Nicotinic acid and niacinamide are used in a variety of therapeutic application as important components of the co-factors, nicotinamide adenine dinucleotide and nicotinamide adenine dinucleotide phosphate. Decreasing the adverse effects will improve the stability and absorption of nicotinic acid. Nicotinic acid aspartic acid dipeptide and tetrapeptide were synthesized via Fmoc solid-phase synthesis, purified via reversed-phase high performance liquid chromatography and characterized via proton and 13C nuclear magnetic resonance and electrospray ionization mass spectrometry to change the property of nicotinic acid for promoting application of niacin derivatives. The interactions of nicotinic acid and nicotinoyl aspartic acid derivatives with calf thymus DNA were investigated by ultraviolet-visible absorption and fluorescence spectroscopy. The hypochromicity in ultraviolet spectra of DNA with increasing of nicotinic acid and derivatives concentration was observed. The fluorescence quenching of nicotinic acid and derivatives to ethidium bromide-DNA was mixture mode according to the Stern-Volmer equation. The results indicated that the interaction modes of nicotinic acid and nicotinoyl derivatives with calf thymus DNA were mixed mode of electrostatic repulsion and embed interaction, and the interaction of derivatives with calf thymus DNA was weakened by the carboxyl number of aspartic acids. Bioavailability and adverse event potential of the synthesized nicotinoyl aspartic acid di and tetrapeptides required to be evaluated.
منابع مشابه
N-terminal extension of sweet peptides in relation to the structural features of peptide sweeteners.
Sweet aspartyl di- and tripeptide esters were extended toward the N-terminus in relation to the structural features of sweet peptides. The sweet peptides were designed on the basis of the receptor site model. It was found that an extension of the sweet aspartyl dipeptide esters by adding a small D-amino acid residue mostly gave sweet compounds (e.g., D-Ala-L-Asp-D-Ala-OMe), although this signif...
متن کاملPreparation of Nicotinoyl Amino Acid Derivatives by Fmoc-solid Phase Synthesis and Preliminary Studies on the Dna-binding Properties of Nicotinoyl Derivatives
Three types of nicotinoyl amino acids, i.e., nicotinoyl leucine (NA-Leu), NA-Leu-His, and NA-Tyr-Tyr, were synthesized by Fmoc solid-phase peptide synthesis, purified by reversed-phase HPLC, and characterized by 1H, 13C NMR and ESI-MS. The interactions of nicotinic acid and nicotinoyl derivatives with ctDNA were investigated by fluorescence spectroscopy. NA-Leu-His and NA-Tyr-Tyr exhibited high...
متن کاملTripeptide arginyl-glycyl-aspartic acid (RGD) for delivery of Cyclophosphamide anticancer drug: A computational approach
Density functional theory (DFT) calculations were performed on tripeptide arginyl-glycyl-aspartic acid (RGD) as an efficient drug carrier to deliver the commercially famous cyclophosphamide (CP) anticancer drug within ethanol solution. The most negative binding energy (-5.22 kcal/mol) was measured for the CP-RGD-7 created through the H-bond interaction between the P=O (phosphoryl) oxygen atom o...
متن کاملDesigning a new tetrapeptide to inhibit the BIR3 domain of the XIAP protein via molecular dynamics simulations
The XIAP protein is a member of apoptosis proteins family. The XIAP protein plays a central role in the inhibition of apoptosis and consists of three Baculoviral IAP Repeat domains. The BIR3 domain binds directly to the N-terminal of caspase-9 and therefore it inhibits apoptosis. N-terminal tetrapeptide region of SMAC protein can bind to BIR3, inhibit it and subsequently induce apoptosis. In th...
متن کاملSynthesis and Functionalization of Gold Nanoparticles by Using of Poly Functional Amino Acids
Synthesis and characterization of two functionalized gold nanoparticles by using of two poly functional amino acids (L-Arginine and L-Aspartic acid) are reported. The gold nanoparticles were reduced by sodium citrate and functionalized with L-Arginine at the pH of 7 and 11 and L-Aspartic acid at the pH of 7. Transmission electron microscopy, UV-Vis spectroscopy, dynamic light scattering, zeta p...
متن کامل