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The synergism of CeCl₃ (Ce) with cysteine (Cys) on the corrosion of P110 carbon steel in 3% NaCl solutions was investigated by electrochemical methods and surface analysis. The results showed that CeCl₃ and cysteine do little to inhibit the corrosion of carbon steel, but the combination of CeCl₃ with cysteine has obvious synergistic effect on the corrosion of carbon steel and the corrosion inhibition efficiency was improved significantly. The potentiodynamic polarization curves indicated that the mixture of CeCl₃ and cysteine acts as a cathodic inhibitor. Scanning electron microscope (SEM) and Infrared (IR) reflection spectra showed the synergistic inhibition effect was formed by the complexes between rare earth Ce(III) ion and amino acid.

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Molecular imprinting is one of few general, nonbiological methods for creating molecular receptors, but the progress in molecular imprinting calls for the predictive tools capable of understanding molecular level complexities of these processes. Thus, computational chemistry which predicts the suitability of functional monomer in designing the sensor for a particular analyte was attempted to design an amino acid (L-serine) sensor based on the molecular imprinting approach using density functional theory (DFT). Here, the computations were carried out to check the feasibility of best suited monomers for imprinting an amino acid (L-serine) in water and allied solvents.

DFT method was utilized at B3LYP/6-31$++$G(d,p) level to optimize template, monomers and template-monomer complexes and basis set superposition error (BSSE) was corrected by means of the counterpoise (CP) method for complexes in gas phase. All monomers can be utilized for imprinting. 2-vinyl pyridine and acrylamide were found to be good for imprinting serine in water but toluene was found to be good porogen for imprinting serine with functional monomer acrylamide. This study will aid in designing a water-compatible MIP sensor for serine molecules, which could be a biomarker for certain neurological disorders.

We present the proof for the source of exchange flying ring of the biological bosonic state in homochirality of L-amino acids. It is a source of knot in parallel transport of Yang–Mills field in genetic code evolved from natural selection. It serves as a source of protein folding structure in L-amino acids over all the protein structure of a living organism. In the proof, we modified Frank’s model for homochirality and added more properties of nonlinearity and supersymmetry. The mirror symmetries transform their left and right homochiral hidden states of reversed reaction over Frank’s equation for spontaneous autocatalysis. We also change the rate of reaction in the model from the Euclidean norm to Minkowski metric with Lorentz invariant in special relativity theory. The speed of light in Minkowski space in this model is an analogy with a source of all species of all living organisms with common 20 L-amino acids as their constituents. The result of the proof agrees with the existence of L-amino acids in nature. By long-term of evolution, the number of concentration of left homochirality is more than the concentration of right homochirality in amino acids propositional to the Chern–Simons current.

Novel 9-proparylcarbazole monomers containing amino acid moieties, 2-N-(tert-butoxycarbonyl)-L-alanine-9-proparylcarbazole ester (1), 2-N-(tert-butoxycarbonyl)-L-O-cyclohexyl-L-glutamic acid-9-proparylcarbazole ester (2) and 2-N-(tert-butoxycarbonyl)-L-phenylalanine-9-proparylcarbazole ester (3) were synthesized and polymerized with (nbd)Rh⁺ [η⁶-C₆H₅B^–(C₆H₅)₃] to give the corresponding polymers with number-average molecular weights ranging from 7050 to 10500 in 70%–86% yields. The polymers were completely soluble in toluene, CHCl₃, CH₂Cl₂, THF and DMSO, but insoluble in hexane, diethyl ether and MeOH. The specific rotation studies revealed that poly(1)–poly(3) do not took predominantly one-handed helical structures in the solvents although they possess chiral groups. The polymers emitted fluorescence in 0.40%–2.35% quantum yields. The cyclic voltammograms of the polymers indicated that the polymers exhibited electrochemical properties.

In addition to controlling the structure of multi-chromophoric arrays, monitoring the spatial orientation of the chromophores in artificial light harvesting devices is a challenge of growing interest. We report in this article our recent advances in this field. It is expected that a better understanding of the physicochemical properties of rigid cofacial porphyrinic tweezers and an identification of the factors governing them will be crucial for the design and the elaboration of new nano-molecules endowed with original properties. Extended multi-porphyrinic architectures, polypeptides bearing pendant porphyrins have been synthesized as linear devices, and a star-like pentaporphyrin as an arborescent array. The structure and the original conformation of the latter confer to this system an unusual duality in its physicochemical properties.

meso-Tris(3,5-di-tert-butylphenyl)porphyrin (P-H) is bonded with L-phenylalanine (H-Phe-OH) directly at the unsubstituted meso-position of the former and the p-position of phenyl group of the latter to afford chiral porphyrin-amino acid conjugate H-Phe(p-P)-OH. The N-(9-fluorenyl)-methyloxycarbonyl compound, Fmoc-Phe(p-P)-OH, was synthesized without any loss of enantiomeric purity (based on chiral HPLC analysis) from commercially available L-tyrosine and was useful for preparation of the peptides in both liquid and solid phases. Other meso-tetraarylporphyrins possessing multi-amino acid moieties are reported, as well as achiral porphyrin-amino acids readily prepared and their dipeptidyl porphyrin dyads.

A samarium hybrid with porphyrin and amino acid as mixed ligands {[Sm(His)(H₂O)][Sm(H₃O)₃](H₂TPPS)₂} • 5H₂O (1) (His = histidine; H₆TPPS = tetra(4-sulfonatophenyl)porphyrin) has been synthesized via a hydrothermal reaction and characterized by single-crystal X-ray diffraction. Compound 1is crystallized in the space group $P\bar{\mathrm{ı}}$ of the triclinic system. Compound 1is characteristic of a three-dimensional (3-D) open framework with the samarium ions in two types of coordinating environments and a saddle-distorted nonplanar porphyrin macrocycle. Compound 1 exhibits fluorescence in the red region. The fluorescence lifetime of 1 is 15.65 ns and the emission quantum yield is 4.1%. The CV/DPV, UV-vis and FT-IR are also reported in detail.

Tetraphyrins(1.1.1.1) (Porphyrins) were merged with amino acids forming a direct bond between a meso-position of macrocycle and a nitrogen available in the side chain of the amino acid. The following intramolecular fusion observed for a free base porphyrin forms a structure with extended $\pi$-delocalisation on the additional carbocyclic fragment, that substantially modifies the observed absorption and emission. A further modulation of electron behaviour has been observed for a deprotonated form of the fused system. A nitrogen atom introduced into the system can be treated as a switching factor that controls the delocalisation significantly influencing the emission by shifting between the available amine and imine tautomeric forms.

The phosphorylation and de-phosphorylation reactions in the cell, through which the bio-energy is released from ATP hydrolysis in biological systems, are described in this paper. Firstly, the bio-energy is accepted by the vibrational amides in protein molecules in virtue of resonant mechanism of frequency or energy, and can transport along the protein molecules in soliton, which is formed by self-trapping of vibrational quantum (or exciton), by means of dipole–dipole interaction among the neighboring peptide groups (or amino acids). Theory and properties of bio-energy transport were proposed and described by many researchers. We here reviewed mainly the theories and features of Davydov's and Pang's models. However these theoretical models including Davydov's and Pang's model were all established based on a periodic and uniform proteins, which are different from practically biological proteins molecules. Therefore, it is necessary to inspect and verify the validity of the theory of bio-energy transport in real biological protein molecules. These problems were extensively studied by a lot of researchers using different methods in past thirty years, a considerable number of research results were obtained. I review here the situation and progresses of study on this problem, in which we reviewed the correctness of the theory of bio-energy transport including Davydov's and Pang's model and its investigated progresses under influences of structural non-uniformity and disorder, side groups and imported impurities of protein chains as well as the thermal perturbation and damping of medium arising from the biological temperature of the systems. The structural non-uniformity arises from the disorder distribution of sequence of masses of amino acid residues, side groups and imported impurities, which results in the changes and fluctuations of the spring constant, dipole–dipole interaction, exciton–phonon coupling constant, diagonal disorder or ground state energy and chain–chain interaction of the molecular channels in the dynamic equations in different models. The influences of structural non-uniformity, side groups and imported impurities as well as the thermal perturbation and damping of medium on the bio-energy transport in the proteins with single chain and three chains were studied by different numerical simulation techniques and methods including the average Hamiltonian way of thermal perturbation, fourth-order Runge–Kutta method, Monte Carlo method, quantum perturbed way and thermodynamic and statistical method, and so on. In this review, the numerical simulation results of bio-energy transport in uniform protein molecules, the influence of structural non-uniformity on the bio-energy transport, the effects of system temperature on the bio-energy transport and the simultaneous effects of structural non-uniformity, damping and thermal perturbation of proteins on the bio-energy transport in single chains and α-helical molecules were included and studied, respectively. The results obtained from these studies and reviews suggest that Davydov's soliton is unstable, but Pang's soliton is stable at physiologic temperature 300 K under influences of structural non-uniformity and disorder, side groups, imported impurities and damping of medium. Thus we can conclude that the soliton in Pang's model is exactly a carrier of the bio-energy transport and Pang's theory is appropriate to α-helical protein molecules. Finally we provided a few of experimental evidences for real existence of the soliton and validity of the theory of bio-energy transport in proteins and stated further the applications of the theory in living systems.

Nano-hydroxyapatite crystals of different morphologies were synthesized by adding two types of amino acids (glycine and arginine) under hydrothermal conditions. The XRD, FTIR, and TEM characterizations of samples showed that the final product was pure hydroxyapatite with high crystallinity. Organic small-molecule amino acids exhibited a significant inhibitory effect on crystal growth during the synthesis process. This regulatory effect is related to the side chains of amino acids. The results of co-culturing with bone mesenchymal stem cells showed that the cell compatibility of nanoparticles differs based on their morphologies. The results of this study are significant for the fabrication of nano-hydroxyapatite with tunable morphology, which can have applications in the fields of bone repair and drug loading.

The optical absorption spectra of complex of Praseodymium in different solvents i.e water, Methanol, Ethanol & Acetic Acid have been recorded in visible region (360-620 nm for Pr³⁺) using amino acid as primary ligand and diol as secondary ligand. The value of energies & intensities of various transitions have been calculated using Judd-Ofelt relation is in good agreement with experimental result. The study of complex found it to be covalent in nature. The spectra in visible region have been recorded on model uv-2601 Rayleigh analytical instrument corp.

In this study, the adsorption differences of different kinds of amino acids (acidic Lglutamic acid (L-Glu), neutral L-threonine (L-Thr) and alkaline L-histidine (L-His)) onto calcium oxalate monohydrate (COM) and calcium oxalate dihydrate (COD) crystals with sizes of 50 nm, 100 nm, 1 μm, 3 μm and 10 μm were investigated using spectrophotometry. The study of adsorption differences of amino acids on calcium oxalate has rarely been conducted; hence, we studied it with different pH values onto COM and COD crystals. The amount of adsorbed amino acids was determined using the depletion method and the centrifugation method was applied. At pH=7.3, COM crystals mainly adsorbed acidic L-Glu and have less adsorption to L-Thr and L-His, while COD mainly adsorbed alkaline L-His. Results of this study showed that when the size of crystal increases, the adsorption amount of crystals decreased. This was attributed to the decreases of specific surface area of larger crystals. The adsorption amount of COM was greater than that of COD with the same size because the specific surface area of COM is greater than COD. Our results help to further illustrate the formation mechanism of calcium oxalate stones and provide inspiration for inhibiting its recurrence.