In Situ Monitoring of Fluorescent Polymer Brushes by Angle-Scanning Based Surface Plasmon Coupled Emission.

Fluorescent polymers have attracted interest in many fields such as sensing, diagnostics, imaging, and organic electronic devices. Real-time techniques to monitor and understand the polymerization process are important for obtaining controllable fluorescence polymers. We present a new technique to in situ monitor the growth process of fluorescent polymer brushes by using angle-scanning based surface plasmon coupled emission (AS-SPCE) approach during electrochemically mediated atom-transfer radical polymerization. The polymer thickness was determined by modeling the location of SPCE emission angle(s) with theoretical calculation. The advantages of unique angle distribution patterns, thickness dependence and effective background rejection of AS-SPCE guarantee the success in the real-time investigation for controllable fabrication of fluorescent polymers.

Correction: Pyrido[1,2-a]pyrimidinium ions - a novel bridgehead nitrogen heterocycles: synthesis, characterisation, and elucidation of DNA binding and cell imaging properties.

Correction for 'Pyrido[1,2-a]pyrimidinium ions - a novel bridgehead nitrogen heterocycles: synthesis, characterisation, and elucidation of DNA binding and cell imaging properties' by Susanta Kumar Manna et al., Org. Biomol. Chem., 2015, 13, 8037-8047.

Pyrido[1,2-a]pyrimidinium ions--a novel bridgehead nitrogen heterocycles: synthesis, characterisation, and elucidation of DNA binding and cell imaging properties.

A novel class of bridgehead nitrogen heterocycles, pyrido[1,2-a]pyrimidinium ions, has been readily synthesized by a two-step one-pot reaction in high yields (up to 93%). These ionic compounds are bench stable and moisture tolerant and have highly fluorescent properties (quantum yield up to 0.65). A characteristic bright bluish fluorescence was observed in polar solvents such as acetonitrile and fluorescent intensity gradually diminishes with decreasing the polarity of the medium, which becomes almost negligible in toluene. These compounds also show interesting bioactivity. DNA interaction, imaging, and viability experiments with human leukemic Jurkat and KG-1A cells revealed that they are potential candidates for cancer diagnosis.

Location and binding mechanism of an ESIPT probe 3-hydroxy-2-naphthoic acid in unsaturated fatty acid bound serum albumins.

The binding site and the binding mechanism of 3-hydroxy-2-naphthoic acid (3HNA) in oleic acid (OA) bound serum albumins (bovine serum albumin (BSA) and human serum albumin (HSA)) have been determined using steady state and time resolved emission of tryptophan residues (Trp) in proteins and the ESIPT emission of 3HNA. Time resolved anisotropy of the probe 3HNA and low temperature phosphorescence of Trp residues of BSA in OA bound BSA at 77K reveals a drastic change of the binding site of 3HNA in the ternary system compared to that in the free protein. 3HNA binds near Trp213 in the ternary system whereas 3HNA binds near Trp134 in the free protein. The structure of OA bound BSA generated using docking methodology exhibits U-bend configuration of all bound OA. The docked pose of 3HNA in the free protein and in OA bound albumins (ternary systems) and the concomitant perturbation of the structure of proteins around the binding region of 3HNA corroborate the enhanced ESIPT emission of 3HNA and the energy transfer efficiency from the donor Trp213 of BSA to 3HNA acceptor in 3HNA-OA-BSA system.

A comparative study of interaction of tetracycline with several proteins using time resolved anisotropy, phosphorescence, docking and FRET.

A comparative study of the interaction of an antibiotic Tetracycline hydrochloride (TC) with two albumins, Human serum albumin (HSA) and Bovine serum albumin (BSA) along with Escherichia Coli Alkaline Phosphatase (AP) has been presented exploiting the enhanced emission and anisotropy of the bound drug. The association constant at 298 K is found to be two orders of magnitude lower in BSA/HSA compared to that in AP with number of binding site being one in each case. Fluorescence resonance energy transfer (FRET) and molecular docking studies have been employed for the systems containing HSA and BSA to find out the particular tryptophan (Trp) residue and the other residues in the proteins involved in the binding process. Rotational correlation time (θc) of the bound TC obtained from time resolved anisotropy of TC in all the protein-TC complexes has been compared to understand the binding mechanism. Low temperature (77 K) phosphorescence (LTP) spectra of Trp residues in the free proteins (HSA/BSA) and in the complexes of HSA/BSA have been used to specify the role of Trp residues in FRET and in the binding process. The results have been compared with those obtained for the complex of AP with TC. The photophysical behaviour (viz., emission maximum, quantum yield, lifetime and θc) of TC in various protic and aprotic polar solvents has been determined to address the nature of the microenvironment of TC in the protein-drug complexes.

Tuning of "antenna effect" of Eu(III) in ternary systems in aqueous medium through binding with protein.

A simple ternary system containing a protein [human serum albumin (HSA)/bovine serum albumin (BSA)], tetracycline hydrochloride (TC), and Eu(III) in suitable aqueous buffer medium at physiological pH (= 7.2) has been shown to exhibit highly efficient "antenna effect" compared to the binary complex of TC with Eu(III) (Eu(3)TC). The ternary system containing E. coli alkaline phosphatase (AP), TC, and Eu(III), however, shows a slight enhancement of Eu(III) emission, although the binding constant of AP with TC is 2 orders of magnitude greater than with BSA/HSA. The enhanced emission of bound TC in the binary systems containing proteins and TC gets quenched in the ternary systems containing HSA/BSA, showing the efficient energy transfer (ET) from TC to Eu(III). Steady state and time-resolved emission studies of each component in all the ternary systems in H(2)O and in D(2)O medium reveal that Eu(III) is very well protected from the O-H oscillator in the ternary system containing HSA/BSA compared to that containing AP. The docking studies locating the binding site of TC in the proteins suggest that TC binds near the surface of AP. In the case of HSA/BSA, TC resides in the interior of the protein resulting in a large shielding effect of Eu(III). The rotational correlation time (θ(c)) determined from the anisotropy decay of bound TC in the complexes and the accessible surface area (ASA) of the ligand in the complexes obtained from the docking studies also support the contention that Eu(3)TC is more exposed to solvent in the case of the ternary system consisting of AP, TC, and Eu(III). The calculated radiative lifetime and the sensitization efficiency ratio of Eu(III) in all the systems clearly demonstrate the protein mediated tuning of "antenna effect" in Eu(III).

Interaction of multitryptophan protein with drug: an insight into the binding mechanism and the binding domain by time resolved emission, anisotropy, phosphorescence and docking.

The interaction of antibiotic Tetracycline hydrochloride (TC) with Alkaline Phosphatase (AP) from Escherichia coli, an important target enzyme in medicinal chemistry, having tryptophan (Trp) residues at 109, 220 and 268 has been studied using the steady state and time resolved emission of the protein and the enhanced emission of the bound drug. The association constant at 298 K (≈10(6) [M](-1)) and the number of binding site (=1) were estimated using the quenched Trp emission of AP, the enhanced emission and the anisotropy of the bound drug. The values of ΔH(0) and ΔS(0) are indicative of electrostatic and H-bonding interaction. The low temperature phosphorescence of free AP and the protein- drug complex and molecular docking comprehensively prove the specific involvement of partially exposed Trp 220 in the binding process without affecting Trp 109 and Trp 268. The Förster energy transfer (ET) efficiency and the rate constant from the Trp residue to TC=0.51 and ≈10(8) s(-1) respectively. Arg 199, Glu 219, Trp 220, Lys 223, Ala 231, Arg 232 and Tyr 234 residues are involved in the binding process. The motional restriction of TC imposed by nearby residues is reflected in the observed life time and the rotational correlation time of bound TC.

Protein-mediated efficient synergistic "antenna effect" in a ternary system in D2O medium.

A ternary system consisting of a protein, catechin (either + or - epimer), and Tb(III) in suitable aqueous buffer medium at physiological pH (= 6.8) has been shown to exhibit highly efficient "antenna effect". Steady state and time-resolved emission studies of each component in the binary complexes (protein with Tb(III) and (+)- or (-)-catechin with Tb(III)) and the ternary systems along with the molecular docking studies reveal that the efficient sensitization could be ascribed to the effective shielding of microenvironment of Tb(III) from O-H oscillator and increased Tb-C (+/-) interaction in the ternary systems in aqueous medium. The ternary system exhibits protein-mediated efficient antenna effect in D(2)O medium due to synergistic ET from both the lowest ππ* triplet state of Trp residue in protein and that of catechin apart from protection of the Tb(III) environment from matrix vibration. The simple system consisting of (+)- or (-)-catechin and Tb(III) in D(2)O buffer at pH 6.8 has been prescribed to be a useful biosensor.