Biomedical subjects

H A Tajmir-Riahi

Publications and source records attributed to H A Tajmir-Riahi.

At least 19 recordsLinked to original sources

PubMed1999

Structural analysis of DNA-chlorophyll complexes by Fourier transform infrared difference spectroscopy.

Porphyrins and metalloporphyrins are strong DNA binders. Some of these compounds have been used for radiation sensitization therapy of cancer and are targeted to interact with cellular DNA. This study was designed to examine the interaction of calf thymus DNA with chlorophyll a (CHL) in aqueous solution at physiological pH with CHL/DNA(phosphate) ratios (r) of 1/160, 1/80, 1/40, 1/20, 1/10, and 1/5. Fourier transform infrared (FTIR) difference spectroscopy was used to characterize the nature of DNA-pigment interactions and to establish correlations between spectral changes and the CHL binding mode, binding constant, sequence selectivity, DNA secondary structure, and structural variations of DNA-CHL complexes in aqueous solution. Spectroscopic results showed that CHL is an external DNA binder with no affinity for DNA intercalation. At low pigment concentration (r = 1/160, 1/80, and 1/40), there are two major binding sites for CHL on DNA duplex: 1) Mg-PO2 and 2) Mg-N7 (guanine) with an overall binding constant of K = 1.13 x 10(4) M-1. The pigment distributions are 60% with the backbone PO2 group and 20% with the G-C base pairs. The chlorophyll interaction is associated with a major reduction of B-DNA structure in favor of A-DNA. At high chlorophyll content (r = 1/10), helix opening occurs, with major spectral alterations of the G-C and A-T bases. At high chlorophyll concentration (1/5), pigment aggregation is observed, which does not favor CHL-DNA complexation.

Animals↗

PubMed1998

Interaction of cisplatin with human serum albumin. Drug binding mode and protein secondary structure.

Cis-diamminedichloroplatinum(II) (cisplatin) is an antitumor drug, which forms intrastrand cross-links DNA adducts. Protein interaction with cisplatin-DNA complexes induces DNA bending and biopolymer structural changes. This study is designed to examined the interaction of cisplatin with human serum albumin (HSA) in aqueous solution at physiological pH with drug concentrations of 0.0001 mM to 0.1 mM, and HSA (fatty acid free) concentration of 2% w/v. Absorption spectra and Fourier transform infrared (FTIR) spectroscopy with its self-deconvolution and second derivative resolution enhancement, as well as curve-fitting procedures, were used to determine the drug binding mode, drug binding constant and the protein secondary structure in aqueous solution. Spectroscopic evidence showed that at low drug concentration (0.0001 mM), minor cisplatin-protein interaction occurs, while at higher drug content (0.001 mM), major Pt-HSA complexation takes place via protein C=O, C-N and S-H donor groups with overall binding constant K = 8.52 x 10(2) M-1. At high drug concentration, cisplatin binding results in major protein secondary structural changes from that of the alpha-helix 55% (free HSA) to 45% and beta-sheet 22% (free HSA) to 32%, in the cisplatin-HSA complexes. The observed spectral changes indicate a partial unfolding of the protein structure, in the presence of cisplatin at high drug concentrations.

Binding Sites↗

PubMed1998

RNA-ascorbate interaction.

Ascorbic acid and divalent iron salts have been widely used to investigate the effects of reactive oxygen species in different biological targets such as nucleic acids, proteins and lipids. This study was designed to examine the interaction of yeast RNA with vitamin C in aqueous solution at physiological pH with drug/RNA(P)(P=phosphate) molar ratios of r=1/80, 1/40, 1/20, 1/10, 1/4 and 1/2. Absorption spectra and Fourier transform infrared (FTIR) difference spectroscopy were used to determine the ascorbate binding mode, binding constant, sequence selectivity and RNA secondary structure in aqueous solution. Spectroscopic evidence showed that at low drug concentration (r=1/80 and 1/40), no major ascorbate-RNA interaction occurs, while at higher drug concentrations (r>1/40), a major drug-RNA complexation was observed through both G-C and A-U base pairs and the backbone phosphate groups with k=31.80 M(-1). Evidence for this comes from large perturbations of the G-C vibrations at 1698 and 1488 cm(-1) and the A-U bands at 1654 and 1608 cm(-1) as well as the phosphate antisymmetric stretch at 1244 cm(-1). At r>1/10, minor structural changes occur for the ribose-phosphate backbone geometry with RNA remaining in the A-family structure. The drug distributions around double helix were about 55% with G-C, 33% A-U and 12% with PO2 groups. A comparison between ascorbate-RNA and ascorbate-DNA complexes showed minor differences. The ascorbate binding (H-bonding) is via anion CO and OH groups.

Ascorbic Acid↗

PubMed1997

RNA-diethylstilbestrol interaction studied by Fourier transform infrared difference spectroscopy.

Diethylstilbestrol (DES), a synthetic estrogen, is known to be a carcinogen in human and in animals. This study was designed to examine the interaction of DES with yeast RNA in aqueous solution at physiological pH with drug/RNA-phosphate (P) molar ratios of 1/80, 1/40, 1/20, 1/10, 1/4, and 1/2. Fourier transform infrared (FTIR) difference spectroscopy was used to determine the drug binding mode, the binding constant, the sequence selectivity, and RNA secondary structure in the RNA.DES complexes. Spectroscopic evidence showed that at low drug concentration (1/80 and 1/40), DES is intercalating through both Gua-Cyt and Ade-Urd base pairs with minor interaction with the backbone PO2 group (external binding). The calculated binding constant of K approximately 8.5 x 10(4) M-1 at a drug concentration of 3.12 x 10(-4) M shows that DES is a weaker intercalator than those of the methylene blue, acridine orange, and ethidium bromide. At high drug content (r > 1/40, where r represents the DES/RNA-phosphate molar ratio), a partial helix destabilization occurs with no alteration of RNA conformation upon drug complexation. However, a comparison with DNA.DES complexes showed that drug intercalation causes major reduction of the B-DNA structure in favor of A-DNA with no participation of the backbone PO2 group in the DES. DNA complexation.

DNA↗

PubMed1997

The effects of spermine and spermidine on the structure of photosystem II proteins in relation to inhibition of electron transport.

Polyamines (PAs) are ubiquitous in cells of higher plants and play an important role in many biological functions. Because PAs affect photosynthetic oxygen evolution, this study is designed to investigate the interaction of spermine (Spm) and spermidine (Spd) cations with proteins of photosystem II (PSII) using PSII-enriched submembranes fraction with polyamine concentrations of 0.01-10 mM. Fourier transform infrared (FTIR) difference spectroscopy with its self-deconvolution and second derivative resolution enhancement as well as curve-fitting procedures was applied, in order to determine the cation binding mode, the protein conformational changes and the structural properties of cation-protein complexes. It is shown that at low polyamine concentration, cation-protein interaction (H-bonding) is through the polypeptide C=O groups with no major perturbation of the protein secondary structure. As cation concentration increases, the polyamine complexation causes significant alterations of the protein secondary structure with a decrease of the alpha-helical domains from 47% (uncomplexed PSII) up to 37% (cation complexes) and an increase in the beta-sheet structure from 18% (uncomplexed PSII) up to 29% (cation complexes). Correlations between the effects of polyamines on protein secondary structure and on the rate of oxygen evolution in PSII are also established.

Cations↗

PubMed1996

Diethylstilbestrol-DNA interaction studied by Fourier transform infrared and Raman spectroscopy.

The interaction of diethylstilbestrol (DES) with calf thymus DNA was investigated at physiological pH with drug/DNA (phosphate) molar ratios (r) of 1:40, 1:20, 1:10, 1:4, 1:2, and 1. Fourier transform infrared and laser Raman difference spectroscopy were used to establish correlations between spectral changes and drug binding mode, sequence selectivity, DNA conformation, and structural properties of DES.DNA complexes in aqueous solution. Spectroscopic results indicated that DES is a weak intercalator with affinity for A-T-rich regions. It is also a groove binder with a major interaction with the thymine O-2 atom. At low drug concentration (r = 1:40), the A-T-rich region is the main target of drug intercalation, while at a higher drug content (r > 1:5), external binding to the G-C bases also occurs with a partial helix destabilization. Evidence for this comes from the spectral alterations of the A-T vibrational frequencies at 1661 cm-1 (Raman) and 1663 and 1609 cm-1 (IR) and of the G-C vibrations at 1581 and 1491 cm-1 (Raman) and 1717 and 1492 cm-1 (IR). Drug intercalation leads to a major reduction of B-DNA structure in favor of A-DNA.

DNA↗

PubMed1996

Aspirin-DNA interaction studied by FTIR and laser Raman difference spectroscopy.

The interaction of calf-thymus DNA with aspirin is investigated in aqueous solution at pH 7-6 with drug/DNA (phosphate) molar ratios of r = 1/40, 1/20, 1/10, 1/5, 1/2, 1 and 2. Fourier transform infrared (FTIR) and laser Raman difference spectroscopy are used to determine drug binding sites, sequence preference and DNA secondary structure, as well as the structural variations of aspirin-DNA complexes in aqueous solution. Spectroscopic evidence showed that at low aspirin concentration (r =1/40), drug-DNA interaction is mainly through the backbone PO2 groups and the A-T base pairs. Such interaction largely perturbs the phosphate vibration at 1222 cm(-1) and the A-T bands at 1663 and 1609 cm(-1) with no major helix destabilization. At higher drug concentration (r > 1/20), the participation of the G-C bases in drug-DNA complexation was evident by strong perturbations of the guanine and cytosine vibrations at 1717 and 1494 cm(-1), with a partial helix destabilization. A major alteration of the B-DNA structure towards A-DNA occurs on drug complexation. The aspirin interaction was through anion CO and COOCH3 donor atoms with those of the backbone PO2 group and DNA bases donor sites (directly or indirectly via H2O molecules).

Animals↗

PubMed1996

An FTIR spectroscopic study of calf-thymus DNA complexation with Al(III) and Ga(III) cations.

The interaction of calf-thymus DNA with trivalent Al and Ga cations, in aqueous solution at pH = 6-7 with cation/DNA(P) (P = phosphate) molar ratios (r) 1/80, 1/40, 1/20, 1/10, 1/4 and 1/2 was characterized by Fourier Transform infrared (FTIR) difference spectroscopy. Spectroscopic results show the formation of several types of cation-DNA complexes. At low metal ion concentration (r = 1/80, 1/40), both cations bind mainly to the backbone PO2 group and the guanine N-7 site of the G-C base pairs (chelation). Evidence for cation chelate formation comes from major shifting and intensity increase of the phosphate antisymmetric stretch at 1222 cm-1 and the mainly guanine band at 1717 cm-1. The perturbations of A-T base pairs occur at high cation concentration with major helix destabilization. Evidence for cation binding to A-T bases comes from major spectral changes of the bands at 1663 and 1609 cm-1 related mainly to the thymine and adenine in-plane vibrations. A major reduction of the B-DNA structure occurs in favor of A-DNA upon trivalent cation coordination.

Aluminum↗

PubMed1995

Does DNA acid fixation produce left-handed Z structure?

The effects of acetic acid (HCOOCH3) on the solution structure of calf-thymus DNA are studied at pH 7.3-2.5 with acid/DNA(P) (phosphate) molar ratios (r) of 1/40, 1/20, 1/10, 1, 2, 10, 20 and 40. Fourier Transform infrared (FTIR) difference spectroscopy is used to establish correlations between spectral changes and base protonation, DNA conformational transition and structural variations of the acid-DNA complexes in aqueous solution. The FTIR difference spectroscopic results showed that protonation of cytosine and subsequent unpairing of the G-C base pairs begins at pH 4-3 and continues up to pH 2.5, where a complete base separation and base unstacking occur. Similarly, protonation of A-T base pairs starts at pH 4-3 and is completed at pH 2.5, where base separation and base unstacking are observed. The protonation of the G-C base pair leads to the formation of Hoogsteen-type H-bonding, before a complete G-C disruption. The biopolymer protonation leads to the formation of several non-B-DNA structures, including left-handed Z conformation.

Animals↗

PubMed1995

A quantitative secondary structure analysis of the 33 kDa extrinsic polypeptide of photosystem II by FTIR spectroscopy.

In chloroplast photosystem II, the extrinsic polypeptide of 33 kDa is involved in the stabilization the Mn cluster in charge of water splitting and in the fulfilment of the Ca(2+)-cofactor requirement for oxygen evolution. The conformational analysis of the purified 33 kDa extrinsic polypeptide was carried out using FTIR spectroscopy with its self-deconvolution and second derivative resolution enhancement as well as curve-fitting procedures. The FTIR spectroscopic results showed that the isolated polypeptide is characterized by a major proportion beta-sheet conformation (36%) with 27% alpha-helix, 24% turn, and 13% beta-antiparallel structures.

Calcium↗

PubMed1995

The effect of HCl on the solution structure of calf thymus DNA: a comparative study of DNA denaturation by proton and metal cations using Fourier transform IR difference spectroscopy.

The interaction of HCl with calf thymus DNA was investigated in aqueous solution at pH 7-2 with H+/DNA(P) (P:phosphate) molar ratios (r) of 1/80, 1/40, 1/20, 1/10, 1/4, 1/2, and 1, using Fourier Transform (FTIR) difference spectroscopy. Correlations between spectral changes, proton binding mode, DNA denaturation, and conformational variations are established. A comparison was also made between the ir spectra of denaturated DNA, in the presence of proton and Cu ions with similar cation concentrations. The FTIR difference spectroscopic results have shown that at low proton concentrations of r = 1/80 and 1/40 (pH 7-5), no major spectral changes occur for DNA, and the presence of H+ results in an increased base-stacking interaction and helical stability. At higher proton concentrations of r > 1/40, the proton binding to the cytosine and adenine bases begins with major destabilization of the helical duplex. As base protonation progresses, a B to C conformational conversion occurs with major DNA spectral changes. Protonation of guanine bases occurs at a high cation concentration r > 1/2 (pH < 3) with a major increase in the intensity of several DNA in-plane vibrations. Copper ion complexation with DNA exhibits marked similarities with proton at high cation concentrations (r > 1/10), whereas at low metal ion concentrations, copper-PO2 and copper-guanine N-7 bindings are predominant. No major DNA conformational transition was observed on copper ion complexation.

Animals↗

PubMed1995

A comparative study of ATP and GTP complexation with trivalent Al, Ga and Fe cations. Determination of cation binding site and nucleotide conformation by FTIR difference spectroscopy.

The interactions of adenosine-5'-triphosphate (Na2H2ATP) and guanosine-5'-triphosphate (Na2H2GTP) with trivalent Al, Ga and Fe cations are investigated in aqueous solution at pH = 6-7 with metal/nucleotide ratios (r) 1/10, 1/2, 1 and 4. Fourier Transform infrared (FTIR) difference spectroscopy is used to characterize the nature of metal cation binding and nucleotide conformational variations, in aqueous solution. Spectroscopic evidences show that at low cation concentration (r = 1/10), metal binding is mainly through the -PO2- and -PO3(2-) groups of the nucleotide moiety (outer-sphere), while at r > 1/10, in addition to direct metal-phosphate binding (chelation), minor metal-base complexes are also formed via indirect metal-NH2 or metal-carbonyl interaction (through H2O). At r = 1, metal macrochelate formation occurs, involving direct cation coordination to phosphate groups and imidazol N-7 atom with an indirect metal-NH2 or metal-carbonyl interaction. At r = 4, polymerization of these metal complexes is observed through nucleotide phosphate chain. The amount of cation/phosphate binding is considerably larger than that of metal/base binding. Evidence for metal-phosphate coordination comes from major spectral changes (shifting and intensity variations) of the alpha-, beta- and gamma-PO2- vibrations in the region 1250-900 cm-1, while metal-base binding is characterized by spectral alterations of the bands at 1700 (guanine carbonyl stretch), 1695 (adenine N-1-H+ mode), 1650-1660 (NH2 bending), 1610-1613 (pyrimidine), 1575 (pyrimidine), 1535-1540 (imidazol), 1470-1480 (imidazol) and 1377 cm-1 (imidazol). The ribose moiety shows C2'-endo/anti conformation for the free ATP and its metal-ATP complexes with an infrared marked band at 821 cm-1. A mixture of both C2'-endo/anti and C3'-endo/anti conformations are occurring for the free GTP and its trivalent metal-complexes with marker bands at 820 and 800 cm-1.

Adenosine Triphosphate↗

PubMed1995

DNA-drug interaction. The effects of vitamin C on the solution structure of Calf-thymus DNA studied by FTIR and laser Raman difference spectroscopy.

The interaction of calf-thymus DNA with L-ascorbic acid was investigated in aqueous solution at pH=7.6 with drug/DNA(P)(P=phosphate) molar ratios (r) of 1/40, 1/20, 1/10, 1/5, 1/2, 1 and 2. Fourier Transform infrared (FTIR) and laser Raman difference spectroscopic techniques were used to establish correlations between spectral modifications and drug binding mode, sequence specificity, DNA melting and conformational changes, as well as structural variations of drug-DNA complexes in aqueous solution. Infrared and Raman spectroscopic results showed that at low drug concentration (r = 1/40), a B to A-type conformational conversion occurs with minor drug-DNA interaction through A-T bases. At r=1/20, drug-PO2 binding was also observed with reduced intensity of DNA inplane vibrational frequencies, due to the increased base-stacking interaction and duplex stability. At r> 1/20, major perturbations of DNA bases were observed for both A-T and G-C base pairs in the major and minor grooves of the duplex. Evidence for this comes form the shift of the infrared and Raman vibrations of the A-T and G-C bases on drug interaction. At r>1/5, a minor helix destabilization occurred with participation of several DNA donor sites in drug complexation. The ascorbate anion interaction occurred mainly through H-bonding of the acid OH and C-O groups with DNA phosphate, bases and doxyribose donor atoms.

Animals↗

PubMed1994

Light-induced Fourier transform infrared spectrum of the cation radical P680+.

The structure of the primary electron donor of photosystem II, P680, is still under debate. It is not decided if it is composed of a chlorophyll (Chl) monomer or dimer. In this study, Fourier transform infrared (FTIR) spectroscopy was used to analyze the changes in the vibration modes occurring upon photooxidation of P680 in a Mn-depleted PS II preparation. It is demonstrated that illumination of the above in the presence of artificial electron acceptors results in a light-minus-dark absorbance change typical of the formation of P680+. The light-minus-dark difference FTIR spectrum obtained under similar conditions is characterized by two negative peaks located at 1694 and 1652 or 1626 cm-1 that can be assigned to the 9-keto groups of the P680 Chl, the latter band being indicative of a strongly associated group. These vibrations are shifted to 1714 and 1676 cm-1, respectively, in the positive features of the difference spectrum attributed to P680+. The occurrence of two pairs of bands attributed to 9-keto groups is discussed in terms of P680 being formed of a Chl dimer.

Chlorophyll↗

PubMed1994

DNA-carbohydrate interaction. The effects of mono- and disaccharides on the solution structure of calf-thymus DNA.

We report the interaction of calf-thymus DNA with D-glucose, D-fructose, D-galactose and sucrose in aqueous solution at physiological pH with sugar/DNA(P)(P = phosphate) molar ratios (r) of 1/10, 1/5, 1, 5 and 10. FTIR difference spectroscopy was used to characterize the nature of sugar-DNA interaction and correlations between spectral changes and structural variations for both sugar and DNA complexes have been established.

Animals↗

PubMed1993

The effects of Cu2+ and Pb2+ on the solution structure of calf thymus DNA: DNA condensation and denaturation studied by Fourier transform ir difference spectroscopy.

The interaction of calf thymus DNA with Cu2+ and Pb2+ was studied in aqueous solution at pH 6.5 with metal/DNA (P) (P = phosphate) molar ratios (r) 1/80, 1/40, 1/20, 1/10, 1/4, 1/2, and 1, using Fourier Transform ir (FTIR) spectroscopy. Correlations between the ir spectral changes, metal ion binding mode, DNA condensation, and denaturation, as well as conformational features, were established. Spectroscopic evidence has shown that at low metal/DNA (P) molar ratios 1/80 and 1/40, copper and lead ions bind mainly to the PO2- of the backbone, resulting in increased base-stacking interaction and duplex stability. The major copper ion base binding via G-C base pairs begins at r > 1/40, while the lead ion base binding occurs at r > 1/20 with the A-T base pairs. The denaturation of DNA begins at r = 1/10 and continues up to r = 1/2 in the presence of copper ions, whereas a partial destabilization of the helical structure was observed for the lead ion at high metal ion concentration (r = 1/2). Metal-DNA binding also results in DNA condensation. No major departure from the B-family structure was observed, upon DNA interaction with these metal ions.

Animals↗

PubMed1993

Interaction of calf-thymus DNA with trivalent La, Eu, and Tb ions. Metal ion binding, DNA condensation and structural features.

The interaction of calf-thymus DNA with La3+, Eu3+ and Tb3+ has been investigated in aqueous solution at pH 6.5, using metal/DNA(P) molar ratios(r) 1/80, 1/40, 1/20, 1/10, 1/4 and 1/2. Correlations between FTIR spectral changes and DNA structural properties have been established. At low metal/DNA(P) (r) 1/80, the metal ions bind mainly to the PO2- groups of the backbone, resulting in increased base-stacking interaction and duplex stability. At (r) 1/40 and 1/20, metal ion binding to the PO2- and the guanine N-7 site (chelation) predominates with minor perturbations of the A-T base pairs. Evidence for this comes from the displacement of the band at 1712 cm-1 (T,G) towards a lower frequency and the PO2- antisymmetric band at 1222 cm-1 towards a higher frequency. At higher metal/DNA(P) ratio, r > 1/20, DNA begins to condensate and drastic structural changes occur, which are accompanied by the shift and intensity changes of several G-C and A-T absorption bands. No major departure from B-DNA conformation was observed before and after DNA condensation even though some local structural modifications were observed. A comparison with the Cu-DNA complexes (denaturated DNA) shows some degree of helical destabilization of the biopolymer in the presence of lanthanide ions.

Animals↗

PubMed1993

The effects of cobalt-hexammine and cobalt-pentammine cations on the solution structure of calf-thymus DNA. DNA condensation and structural features studied by FTIR difference spectroscopy.

The interaction of calf-thymus DNA with cobalt-hexammine and cobalt-pentammine cations was investigated, in aqueous solution at pH 6-7 with cation/DNA(phosphate) molar ratios r = 1/80, 1/40, 1/20, 1/10, 1/4, 1/2 and 1, using Fourier Transform infrared (FTIR) difference spectroscopy. Correlations between spectral changes, DNA condensation and helical stabilization due to the cation interaction as well as conformational features are established. At a very low cation concentration (r = 1/80), the binding of cobalt-hexammine cation with DNA is through the H-bond formation between cation NH3 groups and the PO2 groups of the backbone, resulting in duplex stability. As the cation concentration increases, hydrogen bonding expands towards guanine N-7 and O-6 atoms. At r > 1/20, DNA condensation occurs with major reduction in the intensity of several DNA in-plane vibrations and that of the phosphate group. The cobalt-pentammine cation binding is via the PO2 groups (directly) at very low metal cation concentration (r = 1/80) and the guanine N-7 and the O-6 groups (indirectly) at higher ratios. At r > 1/10, DNA condensation begins with some degree of direct cation-base binding. No major conformational changes from the B-family structure were observed before and after DNA collapse, in the presence of cobalt-ammine cations.

Animals↗