Explore the vast range of titles available.

In this work, the characteristic structure of keratin extracted from two different kinds of industrial waste, namely sheep wool and chicken feathers, using the sulfitolysis method to allow film deposition, has been investigated. The structural and microscopic properties have been studied by means of scanning electron microscopy (SEM), Raman spectroscopy, atomic force microscopy (AFM), and infrared (IR) spectroscopy. Following this, small-angle X-ray scattering (SAXS) analysis for intermediate filaments has been performed. The results indicate that the assembly character of the fiber can be obtained by using the most suitable extraction method, to respond to hydration, thermal, and redox agents. The amorphous part of the fiber and medium range structure is variously affected by the competition between polar bonds (reversible hydrogen bonds) and disulfide bonds (DB), the covalent irreversible ones, and has been investigated by using fine structural methods such as Raman and SAXS, which have depicted in detail the intermediate filaments of keratin from the two different animal origins. The preservation of the secondary structure of the protein obtained does offer a potential for further application of the waste-obtained keratin in polymer films and, possibly, biocomposites.

CP12 is a redox-dependent conditionally disordered protein universally distributed in oxygenic photosynthetic organisms. It is primarily known as a light-dependent redox switch regulating the reductive step of the metabolic phase of photosynthesis. In the present study, a small angle X-ray scattering (SAXS) analysis of recombinant Arabidopsis CP12 (AtCP12) in a reduced and oxidized form confirmed the highly disordered nature of this regulatory protein. However, it clearly pointed out a decrease in the average size and a lower level of conformational disorder upon oxidation. We compared the experimental data with the theoretical profiles of pools of conformers generated with different assumptions and show that the reduced form is fully disordered, whereas the oxidized form is better described by conformers comprising both the circular motif around the C-terminal disulfide bond detected in previous structural analysis and the N-terminal disulfide bond. Despite the fact that disulfide bridges are usually thought to confer rigidity to protein structures, in the oxidized AtCP12, their presence coexists with a disordered nature. Our results rule out the existence of significant amounts of structured and compact conformations of free AtCP12 in a solution, even in its oxidized form, thereby highlighting the importance of recruiting partner proteins to complete its structured final folding.

In land plants and algae, the Calvin–Benson (CB) cycle takes place in the chloroplast, a specialized organelle in which photosynthesis occurs. Thioredoxins (TRXs) are small ubiquitous proteins, known to harmonize the two stages of photosynthesis through a thiol-based mechanism. Among the 11 enzymes of the CB cycle, the TRX target phosphoribulokinase (PRK) has yet to be characterized at the atomic scale. To accomplish this goal, we determined the crystal structures of PRK from two model species: the green alga Chlamydomonas reinhardtii (CrPRK) and the land plant Arabidopsis thaliana (AtPRK). PRK is an elongated homodimer characterized by a large central β-sheet of 18 strands, extending between two catalytic sites positioned at its edges. The electrostatic surface potential of the catalytic cavity has both a positive region suitable for binding the phosphate groups of substrates and an exposed negative region to attract positively charged TRX-f. In the catalytic cavity, the regulatory cysteines are 13 Å apart and connected by a flexible region exclusive to photosynthetic eukaryotes—the clamp loop—which is believed to be essential for oxidation-induced structural rearrangements. Structural comparisons with prokaryotic and evolutionarily older PRKs revealed that both AtPRK and CrPRK have a strongly reduced dimer interface and an increased number of random-coiled regions, suggesting that a general loss in structural rigidity correlates with gains in TRX sensitivity during the molecular evolution of PRKs in eukaryotes.

Single lithium-ion conducting polymer electrolytes are promising candidates for next generation safer lithium batteries. In this work, Li+-conducting Nafion membranes have been synthesized by using a novel single-step procedure. The Li-Nafion membranes were characterized by means of small-wide angle X-ray scattering, infrared spectroscopy and thermal analysis, for validating the proposed lithiation method. The obtained membranes were swollen in different organic aprotic solvent mixtures and characterized in terms of ionic conductivity, electrochemical stability window, lithium stripping-deposition ability and their interface properties versus lithium metal. The membrane swollen in ethylene carbonate:propylene carbonate (EC:PC, 1:1 w/w) displays good temperature-activated ionic conductivities (σ ≈ 5.5 × 10–4 S cm−1 at 60 °C) and a more stable Li-electrolyte interface with respect to the other samples. This Li-Nafion membrane was tested in a lithium-metal cell adopting LiFePO4 as cathode material. A specific capacity of 140 mAhg−1, after 50 cycles, was achieved at 30 °C, demonstrating the feasibility of the proposed Li-Nafion membrane.

The present paper investigated the synthesis of peptide-based hydrogel composites containing photo-generated silver nanoparticles (AgNPs) obtained in the presence and absence of honey as tensile strength enhancer and hydrogel stabilizer. Fmoc-Phe and diphenylalanine (Phe2) were used as starting reagents for the hydrogelator synthesis via an enzymatic method. In particular, we developed an in situ one-pot approach for preparing AgNPs inside peptide hydrogels using a photochemical synthesis, without any toxic reducing agents, with reaction yields up to 30%. The structure and morphology of the nanohybrids were characterized with different techniques such as FESEM, UV-Vis, DLS, SAXS and XPS. Moreover, the antibacterial activity of these hybrid biomaterials was investigated on a laboratory strain and on a clinical isolate of Staphylococcus aureus. Results demonstrated that honey increased both swelling ability and also mechanical stability of the hydrogel. Finally, a higher antibacterial effect of AgNPs in the hybrid was observed in the presence of honey. In particular, AgNPs/hgel and AgNPs/hgel-honey showed an enhanced antibacterial activity (3.12 mg/L) compared to the free form of AgNPs, alone or in combination with honey (6.25 mg/L) for both S. aureus strains.

The photoantibacterial properties of titania nanoparticles (TiO2NPs) are attracting much interest, but the separation of their suspension limits their application. In this study, the encapsulation of commercial TiO2NPs within self-assembling tripeptide hydrogels to form hgel-TiO2NP composites with significant photoantibacterial properties is reported. The Fmoc-Phe3 hydrogelator was synthesized via an enzymatic method. The resulting composite was characterized with DLS, ζ-potential, SAXS, FESEM-EDS and rheological measurements. Two different concentrations of TiO2NPs were used. The results showed that, by increasing the TiO2NP quantity from 5 to 10 mg, the value of the elastic modulus doubled, while the swelling ratio decreased from 63.6 to 45.5%. The antimicrobial efficacy of hgel-TiO2NPs was tested against a laboratory Staphylococcus aureus (S. aureus) strain and two methicillin-resistant S. aureus (MRSA) clinical isolates. Results highlighted a concentration-dependent superior antibacterial activity of hgel-TiO2NPs over TiO2NPs in the dark and after UV photoactivation. Notably, UV light exposure substantially increased the biocidal action of hgel-TiO2NPs compared to TiO2NPs. Surprisingly, in the absence of UV light, both composites significantly increased S. aureus growth relative to control groups. These findings support the role of hgel-TiO2NPs as promising biocidal agents in clinical and sanitation contexts. However, they also signal concerns about TiO2NP exposure influencing S. aureus virulence.

The scientific relevance of quinolines is strictly linked to the fine-tuning of their features by functionalizing the heterocyclic core. Consequently, the compounds of this class are very versatile and can be used as possible drugs for a lot of medical applications. In this work, the inclusion of eight synthetic quinoline derivatives in liposomes formulated with different lipids was investigated in terms of the encapsulation efficiency and to highlight the effect on the liposome size distribution and thermotropic behavior. Excellent encapsulation was accomplished with all the quinoline/phospholipid combinations. Differences in the interactions at the molecular level, dependent on the quinoline molecular scaffolds and lipid structure, were observed, which could significantly bias the interaction with the drug and its release in pharmaceutical applications. Experiments in combination with computational studies demonstrated that the UV absorption of quinolines with expanded conjugation could be affected by the environment polarity. This was probably due to a solvent-dependent ability of these quinolines to stack into aggregates, which could also occur upon inclusion into the lipid bilayer.

CP12 is a redox-dependent conditionally disordered protein universally distributed in oxygenic photosynthetic organisms. It is primarily known as a light-dependent redox switch regulating the reductive step of the metabolic phase of photosynthesis. In the present study, a small angle X-ray scattering (SAXS) analysis of recombinant Arabidopsis CP12 (AtCP12) in a reduced and oxidized form confirmed the highly disordered nature of this regulatory protein. However, it clearly pointed out a decrease in the average size and a lower level of conformational disorder upon oxidation. We compared the experimental data with the theoretical profiles of pools of conformers generated with different assumptions and show that the reduced form is fully disordered, whereas the oxidized form is better described by conformers comprising both the circular motif around the C-terminal disulfide bond detected in previous structural analysis and the N-terminal disulfide bond. Despite the fact that disulfide bridges are usually thought to confer rigidity to protein structures, in the oxidized AtCP12, their presence coexists with a disordered nature. Our results rule out the existence of significant amounts of structured and compact conformations of free AtCP12 in a solution, even in its oxidized form, thereby highlighting the importance of recruiting partner proteins to complete its structured final folding.

Oxygenic phototrophs perform carbon fixation through the Calvin–Benson cycle. Different mechanisms adjust the cycle and the light–harvesting reactions to rapid environmental changes. Photosynthetic glyceraldehyde–3–phosphate dehydrogenase (GAPDH) is a key enzyme of the cycle. In land plants, different photosynthetic GAPDHs exist: the most abundant formed by hetero-tetramers of A and B–subunits, and the homotetramer A4. Regardless of the subunit composition, GAPDH is the major consumer of photosynthetic NADPH and for this reason is strictly regulated. While A4–GAPDH is regulated by CP12, AB–GAPDH is autonomously regulated through the C-terminal extension (CTE) of B–subunits. Reversible inactivation of AB–GAPDH occurs via oxidation of a cysteine pair located in the CTE, and substitution of NADP(H) with NAD(H) in the cofactor binding domain. These combined conditions lead to a change in the oligomerization state and enzyme inactivation. SEC–SAXS and single–particle cryoEM analysis disclosed the structural basis of this regulatory mechanism. Both approaches revealed that (A2B2)n–GAPDH oligomers with n=1, 2, 4 and 5 co–exist in a dynamic system. B–subunits mediate the contacts between adjacent A2B2 tetramers in A4B4 and A8B8 oligomers. The CTE of each B–subunit penetrates into the active site of a B–subunit of the adjacent tetramer, while the CTE of this subunit moves in the opposite direction, effectively preventing the binding of the substrate 1,3–bisphosphoglycerate in the B–subunits. The whole mechanism is made possible, and eventually controlled, by pyridine nucleotides. In fact, NAD(H) by removing NADP(H) from A–subunits allows the entrance of the CTE in B–subunits active sites and hence inactive oligomer stabilization. Competing Interest Statement The authors have declared no competing interest.

In land plants and algae, the Calvin-Benson (CB) cycle takes place in the chloroplast, a specialized organelle in which photosynthesis occurs. Thioredoxins (TRXs) are small ubiquitous proteins, known to harmonize the two stages of photosynthesis through a thiol-based mechanism. Among the 11 enzymes of the CB cycle, the TRX target phosphoribulokinase (PRK) has yet to be characterized at the atomic scale. To accomplish this goal, we determined the crystal structures of PRK from two model species: the green alga Chlamydomonas reinhardtii (CrPRK) and the land plant Arabidopsis thaliana (AtPRK). PRK is an elongated homodimer characterized by a large central β-sheet of 18 strands, extending between two catalytic sites positioned at its edges. The electrostatic surface potential of the catalytic cavity has both a positive region suitable for binding the phosphate groups of substrates and an exposed negative region to attract positively charged TRX-f. In the catalytic cavity, the regulatory cysteines are 13 Å apart and connected by a flexible region exclusive to photosynthetic eukaryotes, the clamp loop, which is believed to be essential for oxidation induced structural rearrangements. Structural comparisons with prokaryotic and evolutionarily older PRKs revealed that both AtPRK and CrPRK have a strongly reduced dimer interface and increased number of random coiled regions, suggesting that a general loss in structural rigidity correlates with gains in TRX sensitivity during the molecular evolution of PRKs in eukaryotes.