An overview of protein-DNA and protein-RNA interactions

Tajmir-Riahi, H.A.

doi:10.1007/bf03245950

Cited by 14 publications

(6 citation statements)

References 34 publications

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“…Similarly, one binding constant was observed for aspirin-HSA, cis-Pt-HSA and aspirin-RNase complexes [43][44][45]. These binding constants are similar to those of the other ligand-protein interactions [46].…”

Section: Stability Of Drug-atpase Complexessupporting

confidence: 61%

Flexibility of Na,K-ATPase secondary structure upon drug-protein interaction

Tajmir-Riahi

2007

JICS

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The enzyme Na + , K + -ATPase is an integral membrane protein which transports sodium and potassium cations against an electrochemical gradient. The transport of Na + and K + ions is connected to an oscillation of the enzyme between the two conformational states, the E 1 (Na + ) and the E 2 (K + ) conformations. The enzymatic activity of ATPase is largley affected by different ligands complexation. This review reports the effects of several drugs such as AZT (anti-AIDS), cis-Pt (antitumor), aspirin (anti-inflammatory) and vitamin C (antioxidant) on the stability and secondary structure of Na,K-ATPase in vitro. Drugenzyme binding is mainly through H-bonding to the polypeptide C=O and C-N groups with two binding constants K 1(AZT) = 5.30 × 10 5 M -1 and K 2(AZT) = 9.80 × 10 3 M -1 for AZT and one binding constant for K cis-Pt = 1.93 × 10 4 M -1 , K aspirin = 6.45 × 10 3 M -1 and K ascorbate = 1.04 × 10 4 M -1 for cis-Pt, aspirin and ascorbic acid. The enzyme secondary structure was altered from that of α-helix 19.8% (free protein) to almost 22-26% and the β-sheet from 25.6% to 18-22%, upon drug complexation with the order of induced stability AZT > cis-Pt > ascorbate > aspirin.

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Section: Stability Of Drug-atpase Complexessupporting

confidence: 61%

Flexibility of Na,K-ATPase secondary structure upon drug-protein interaction

Tajmir-Riahi

2007

JICS

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“…The infrared spectrum of the DNA/Ppy complexes and pure Ppy were performed on Niconet 6700 FT-IR machine with the effective range from 400 cm -1 to 4000 cm -1 at room temperature. As shown in Figure 3, the absorption band at 1889 cm -1 -1629 cm -1 vibration plane implied G-C and A-T base pairs while the backbone phosphate group at 1095 cm -1 was perturbed upon Ppy interaction [17,18].…”

Section: Ftir Spectrum Of Ppy and Dna/ppymentioning

confidence: 97%

Directly immobilized DNA sensor for label-free detection of herpes virus

Tam¹,

Tuan²,

Chien³

2009

JBiSE

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This paper reports the direct immobilization of deoxyribonucleic acid (DNA) sequences of Herpes simplex virus (5’–AT CAC CGA CCC GGA GAG GGA C–3’) on the surface of DNA sensor by using the cyclic voltammetric method with the presence of pyrrole. The potential was scanned from –0.7 volt to + 0.6 volt, the scanning rate was at 100mV/s. This kind of DNA sensor was developed to detect Herpes virus DNA in real samples. The FTIR was applied to verify specific binding of DNA sequence and conducting polymer, the morphology of conducting polymer doped with DNA strands was investigated by using a field emission scanning electron microscope (FE-SEM). The results showed that output signal given by coimmobilized DNA/PPy membrane sensor was better than that given by APTS immobilized membrane sensors. The sensor can detect as low as 2 nM of DNA target in real samples

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“…HSA has only one Trp residue (Trp 214), which is located in a large hydrophobic cavity at subdomain IIA. This residue is dominantly responsible for the intrinsic emission of HAS [22]. Fluorescence spectroscopy studies provide the main information about the binding of a ligand to a receptor.…”

Section: Fluorescence Spectroscopymentioning

confidence: 99%

Exploring The Interactions of a Natural Gamma-Oryzanol with Human Serum Albumin: Surface Plasmon Resonance, Fluorescence, and Molecular Modeling Studies

et al. 2021

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γ-oryzanol (ORY) is the vital bioactive compound, which is a mixture of ferulic acid ester and plant sterols. In the present work, the binding of ORY to human serum albumin (HSA) was investigated at the molecular level using fluorescence spectroscopy and surface plasmon resonance (SPR) as well as molecular modeling studies. Based on the fluorescence data analysis, ORY can form a non-fluorescent complex with HSA and induce static quenching of the emission intensity of HSA. Also, the high value of K SV (34.69 × 104 M−1) confirmed a high sensitivity of HSA toward ORY. The real-time monitoring of the binding of ORY to HSA was carried out using the SPR technique. The small K D value (1.23 × 10−6 M) calculated by SPR analysis indicated a high affinity of ORY toward HSA. The molecular modeling studies confirmed that ORY has only one binding site on HSA and binds HSA in a cavity between subdomain IIA and IIIA.

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An overview of protein-DNA and protein-RNA interactions

Cited by 14 publications

References 34 publications

Flexibility of Na,K-ATPase secondary structure upon drug-protein interaction

Flexibility of Na,K-ATPase secondary structure upon drug-protein interaction

Directly immobilized DNA sensor for label-free detection of herpes virus

Exploring The Interactions of a Natural Gamma-Oryzanol with Human Serum Albumin: Surface Plasmon Resonance, Fluorescence, and Molecular Modeling Studies

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