Electron Beam Processing as a Promising Tool to Decontaminate Polymers Containing Brominated Flame Retardants.

Electron Beam (EB) irradiation was utilized to decontaminate model systems of industrial polymers that contain a brominated flame retardant (BFR). Acrylonitrile-butadiene-styrene (ABS) and Polycarbonate (PC) are two types of polymers commonly found in Waste Electrical and Electronic Equipment (WEEE). In this study, these polymers were exposed to EB irradiation to degrade DecaBromoDiphenylEther (DBDE), one of the most toxic BFRs. Fourier-transform infrared spectroscopy analysis demonstrated an 87% degradation rate of DBDE for the ABS-DBDE system and 91% for the PC-DBDE system following an 1800 kGy irradiation dose. Thermal analysis using Differential Scanning Calorimetry revealed the presence of crosslinking in ABS and a minor reduction in the glass transition temperature of PC after EB processing. Polymers exhibited thermal stability after photolysis, as indicated by thermogravimetric analysis. In summary, EB irradiation had no impact on the overall thermal properties of both polymers. High-resolution mass spectrometry analysis has confirmed the debromination of both ABS-DBDE and PC-DBDE systems. Therefore, the results obtained are promising and could offer an alternative approach for removing bromine and other additives from plastic E-waste.

Degradation processes of brominated flame retardants dispersed in high impact polystyrene under UV-visible radiation.

In order to protect human health and the environment, several regulations have been introduced in recent years to reduce or even eliminate the use of some brominated flame retardants (BFRs) due to their toxicity, persistence and bioaccumulation. Dispersions of these BFRs in polymers are widely used for various applications. In this report, four different brominated molecules, decabromodiphenyl ether (DBDE), hexabromocyclododecane (HBCDD), decabromodiphenyl ethane (DBDPE) and tris(tribromophenoxy)triazine (TTBPT), were dispersed in the solid matrix of an industrial polymer, high impact polystyrene (HIPS). The possibility of degradation of these BFRs within HIPS under UV-visible irradiation in ambient air was investigated. The degradation kinetics of DBDE and HBCDD were followed by Fourier transform infrared spectroscopy (FTIR) and high-resolution two-step laser mass spectrometry (L2MS). The thermal properties of the pristine and irradiated polymer matrix were monitored by thermogravimetric analysis (TGA) and differential scanning calorimetry (DSC), which showed that these properties were globally preserved. Volatile photoproducts from the degradation of DBDE, DBDPE and TTBPT were identified by headspace gas chromatography/mass spectrometry analysis. Under the chosen experimental conditions, BFRs underwent rapid degradation after a few seconds of irradiation, with conversions exceeding 50% for HIPS/DBDE and HIPS/HBCDD systems.

Characterization of Asx Turn Types and Their Connate Relationship with ß-Turns.

Invited for the cover of this issue are David J. Aitken, Michel Mons, and co-workers at Université Paris-Saclay. The image depicts the investigation strategies used to document the intrinsic structures of an important secondary structure in proteins, the so-called Asx turn. Read the full text of the article at 10.1002/chem.202104328.

Isomer Differentiation of Trapped C16H10+ Using Low-Energy Collisions and Visible/VUV Photons.

Polycyclic aromatic hydrocarbons are major species in astrophysical environments, and this motivates their study in samples of astrochemical interest such as meteorites and laboratory analogues of stardust. Molecular analyses of carbonaceous matter in these samples show a dominant peak at m/z = 202.078 corresponding to C16H10. Obtaining information on the associated isomeric structures is a challenge for the molecular analysis of samples available in very small quantities (mg or less). Here we show that coupling laser desorption ionization mass spectrometry with ion trapping opens up the possibility of unraveling isomers by activating ion fragmentation via collisions or photon absorption. We report the best criteria for differentiating isomers with comparable dissociation energies, namely pyrene, fluoranthene, and 9-ethynylphenanthrene, on the basis of the parent dissociation curve and the ratio of dehydrogenation channels. Photoabsorption schemes (multiple photon absorption in the visible range and single photon absorption at 10.5 eV) are more effective in differentiating these isomers than activation by low energy collisions. The impact of the activation scheme on the fragmentation kinetics and dehydrogenation pathways is discussed. By analyzing the 10.5 eV photodissociation measurements with a simple kinetic model, we were able to derive a branching ratio for the H and 2H/H2 loss channels of the parent ions. The results suggest a role in the formation of H2 for bay hydrogens that are present in both fluoranthene and 9-ethynylphenanthrene. In addition, we suggest for the latter the presence of a highly competitive 2H loss channel, possibly associated with the formation of a pentagonal ring.

Selenium in Proteins: Conformational Changes Induced by Se Substitution on Methionine, as Studied in Isolated Model Peptides by Optical Spectroscopy and Quantum Chemistry.

The side-chain of methionine residues is long enough to establish NH⋯S H-bonds with neighboring carbonyl groups of the backbone, giving rise to so-called intra-residue 6δ and inter-residue 7δ H-bonds. The aim of the present article is to document how the substitution of sulfur with a selenium atom affects the H-bonding of the Met system. This was investigated both experimentally and theoretically by conformation-resolved optical spectroscopy, following an isolated molecule approach. The present work emphasizes the similarities of the Met and Sem residues in terms of conformational structures, energetics, NH⋯Se/S H-bond strength and NH stretch spectral shifts, but also reveals subtle behavior differences between them. It provides evidence for the sensitivity of the H-bonding network with the folding type of the Sem/Met side-chains, where a simple flip of the terminal part of the side-chain can induce an extra 50 cm-1 spectral shift of the NH stretch engaged in a 7δ NH⋯S/Se bond.

A theoretical and experimental case study of the hydrogen bonding predilection of S-methylcysteine.

S-containing amino acids can lead to two types of local NH···S interactions which bridge backbone NH sites to the side chain to form either intra- or inter-residue H-bonds. The present work reports on the conformational preferences of S-methyl-L-cysteine, Cys(Me), using a variety of investigating tools, ranging from quantum chemistry simulations, gas-phase UV and IR laser spectroscopy, and solution state IR and NMR spectroscopies, on model compounds comprising one or two Cys(Me) residues. We demonstrate that in gas phase and in low polarity solution, the C- and N-capped model compound for one Cys(Me) residue adopts a preferred C5-C6γ conformation which combines an intra-residue N-H···O=C backbone interaction (C5) and an inter-residue N-H···S interaction implicating the side-chain sulfur atom (C6γ). In contrast, the dominant conformation of the C- and N-capped model compound featuring two consecutive Cys(Me) residues is a regular type I ß-turn. This structure is incompatible with concomitant C6γ interactions, which are no longer in evidence. Instead, C5γ interactions occur, that are fully consistent with the turn geometry and additionally stabilize the structure. Comparison with the thietane amino acid Attc, which exhibits a rigid cyclic side chain, pinpoints the significance of side chain flexibility for the specific conformational behavior of Cys(Me).

An intraresidue H-bonding motif in selenocysteine and cysteine, revealed by gas phase laser spectroscopy and quantum chemistry calculations.

Models of protein chains containing a seleno-cysteine (Sec) residue have been investigated by gas phase laser spectroscopy in order to document the effect of the H-bonding properties of the SeH group in the folding of the Sec side chain, by comparison with recent data on Ser- and Cys-containing sequences. Experimental data, complemented by quantum chemistry calculations and natural bonding orbital (NBO) analyses, are interpreted in terms of the formation of a so-called 5γ intra-residue motif, which bridges the acceptor chalcogen atom of the side chain to the NH bond of the same residue. This local structure, in which the O/S/Se atom is close to the plane of the N-terminal side amide, is constrained by local backbone-side chain hyperconjugation effects involving the S and Se atoms. Theoretical investigations of the Cys/Sec side chain show that (i) this 5γ motif is an intrinsic feature of these residues, (ii) the corresponding H-bond is strongly non-linear and intrinsically weak, (iii) but enhanced by γ- and ß-turn secondary structures, which promote a more favorable 5γ H-bonding approach and distance. The resulting H-bonds are slightly stronger in selenocysteine than in cysteine, but nearly inexistent in serine, whose side chain in contrast behaves as a H-bonding donor. The modest spectral shifts of the Cys/Sec NH stretches measured experimentally reflect the moderate strength of the 5γ H-bonding, in agreement with the correlation obtained with a NBO-based H-bond strength indicator. The evolution along the Ser, Cys and Sec series emphasizes the compromise between the several factors that control the H-bonding in a hyperconjugation-constrained geometry, among them the chalcogen van der Waals and covalent radii. It also illustrates the 5γ H-bond enhancements with the Sec and Cys residues favoured by the constraints imposed by the γ- and ß-turn structures of the peptide chain.

Intrinsic folding of the cysteine residue: competition between folded and extended forms mediated by the -SH group.

A dual microwave and optical spectroscopic study of a capped cysteine amino acid isolated in a supersonic expansion, combined with quantum chemistry modelling, enabled us to characterize the conformational preferences of Cys embedded in a protein chain. IR/UV double resonance spectroscopy provided evidence for the coexistence of two conformers, assigned to folded and extended backbones (with classical C7 and C5 backbone H-bonding respectively), each of them additionally stabilized by specific main-chain/side-chain H-bonding, where the sulfur atom essentially plays the role of H-bond acceptor. The folded structure was confirmed by microwave spectroscopy, which demonstrated the validity of the DFT-D methods currently used in the field. These structural and spectroscopic results, complemented by a theoretical Natural Bond Orbital analysis, enabled us to document the capacity of the weakly polar -CH2-SH side chain of Cys to adapt itself to the intrinsic local preferences of the peptide backbone, i.e., a γ-turn or a ß-sheet extended secondary structure. The corresponding local H-bonding bridges the side chain acceptor S atom to the backbone NH donor site of the same or the next residue along the chain, through a 5- or a 6-membered ring respectively.

Non-covalent interactions reveal the protein chain δ conformation in a flexible single-residue model.

The δ conformation is a local secondary structure in proteins that implicates a πamide N-H⋯N interaction between a backbone N atom and the NH of the following residue. Small-molecule models thereof have been limited so far to rigid proline-type compounds. We show here that in derivatives of a cyclic amino acid with a sulphur atom in the γ-position, specific side-chain/backbone N-H⋯S interactions stabilize the δ conformation sufficiently to allow it to compete with classical C5 and C7 H-bonded conformers.

N-H⋯X interactions stabilize intra-residue C5 hydrogen bonded conformations in heterocyclic α-amino acid derivatives.

Nature makes extensive and elaborate use of hydrogen bonding to assemble and stabilize biomolecular structures. The shapes of peptides and proteins rely significantly on N-H⋯O[double bond, length as m-dash]C interactions, which are the linchpins of turns, sheets and helices. The C5 H-bond, in which a single residue provides both donor and acceptor, is generally considered too weak to force the backbone to adopt extended structures. Exploiting the synergy between gas phase (experimental and quantum chemistry) and solution spectroscopies to decipher IR spectroscopic data, this work demonstrates that the extended C5-based conformation in 4-membered ring heterocyclic α-amino acid derivatives is significantly stabilized by the formation of an N-H⋯X H-bond. In this synergic system the strength of the C5 interaction remains constant while the N-H⋯X H-bond strength, and thereby the support provided by it, varies with the heteroatom.

Conformation control through concurrent N-H⋯S and N-H⋯O[double bond, length as m-dash]C hydrogen bonding and hyperconjugation effects.

In addition to the classical N-H⋯O[double bond, length as m-dash]C non-covalent interaction, less conventional types of hydrogen bonding, such as N-H⋯S, may play a key role in determining the molecular structure. In this work, using theoretical calculations in combination with spectroscopic analysis in both gas phase and solution phase, we demonstrate that both these H-bonding modes exist simultaneously in low-energy conformers of capped derivatives of Attc, a thietane α-amino acid. 6-Membered ring inter-residue N-H⋯S interactions (C6γ), assisted by hyperconjugation between the thietane ring and the backbone, combine with 5-membered ring intra-residue backbone N-H⋯O[double bond, length as m-dash]C interactions (C5) to provide a C5-C6γ feature that stabilizes a planar geometry in the monomer unit. Two contiguous C5-C6γ features in the planar dimer implicate an unprecedented three-centre H-bond of the type C[double bond, length as m-dash]O⋯H(N)⋯SR2, while the trimer adopts two C5-C6γ features separated by a Ramachandran α-type backbone configuration. These low-energy conformers are fully characterized in the gas phase and support is presented for their existence in solution state.