Raman study of prereactional transformations in calcium hydroxide crystals during a thermal treatment leading to dehydration

The Raman spectroscopy study of Ca(OH)₂ single crystals shows that important modifications take place in the crystal structure far below the dehydration temperature. In particular, an intense and broad background scattering and a broad band centered at ～1650 cm^?1 evolve in the Raman spectra.     

Effects of colored noise on the dynamics of quantum entanglement of a one-parameter qubit—qutrit system

We analyzed the effect of colored noise on the negativity dynamics of a hybrid system consisting of a qubit-qutrit and not interacting, prepared from the start in an entangled one-parameter state and acting with noise in local and non-local environments. In this pink and brown noise we investigated two different situations: in the first situation, the noise is produced by a bistable oscillator with an unknown exchange rate; however, in the second situation, the noise is generated by a set of bistable oscillators. We found that entanglement decreases with time to zero, and undergoes the phenomenon of sudden death and rebirth. The pink noise is more prone to entanglement than the brown noise and the non-local environment is more prone to entanglement than the local one. When the number of fluctuators is increased, entanglement decays faster and finally, for certain parameters of the initial state, the subsystems are not affected by the noise.     

Thermal Stabilization of an Endoglucanase by Cyclization

An intein-driven protein splicing approach allowed for the covalent linkage between the N- and C-termini of a polypeptide chain to create circular variants of the endo-??-1,3-1,4-glucanase, LicA, from Bacillus licheniformis. Two circular variants, LicA-C1 and LicA-C2, which have connecting loops of 20 and 14 amino acids, respectively, showed catalytic activities that are approximately two and three times higher, respectively, compared to that of the linear LicA (LicA-L1). The thermal stability of the circular variants was significantly increased compared to the linear form. Whereas the linear glucanase lost half of its activity after 3?min at 65?°C, the two circular variants have 6-fold (LicA-C1) and 16-fold (LicA-C2) increased half-life time of inactivation. In agreement with this, fluorescence spectroscopy and differential scanning calorimetry studies revealed that circular enzymes undergo structural changes at higher temperatures compared to that of the linear form. The effect of calcium on the conformational stability and function of the circular LicAs was also investigated, and we observed that the presence of calcium ions results in increased thermal stability. The impact of the length of the designed loops on thermal stability of the circular proteins is discussed, and it is suggested that cyclization may be an efficient strategy for the increased stability of proteins.     

Synthesis of diamino-furostan sapogenins and their use as scaffolds for positioning peptides in a preorganized form

The synthesis of peptide-furostane conjugates from natural steroidal sapogenins is reported. The approach comprises the introduction of α-oriented amino groups into spirostanic sapogenins followed by reductive opening of the spiroketal chain, thus producing diamino-furostanic scaffolds suitable for further functionalization. Solid and solution-phase coupling processes were utilized for the incorporation of various α-amino acids and peptides into the furostanic skeletons. The attachment position depends on the steroidal sapogenin originally used, i.e., diosgenin or hecogenin. The resulting furostanic skeletons feature a trans A/B-ring fusion and hold the peptides in axial disposition. This characteristic ensures a preorganized alignment of the peptidic motifs, an important structural feature for future applications in molecular recognition and catalysis. A macrocyclic tripeptide-furostane conjugate was also produced by a combination of peptide coupling, Staudinger ligation, and a cyclization protocol. This work constitutes the first report on the use of furostanic sapogenins as scaffolds for positioning natural amino acids and (cyclo)peptides.     

Efficient synthesis of rearranged cholest-13(17)-enes catalysed by montmorillonite-clay

Backbone rearranged cholest-13(17)-enes are obtained quantitatively from cholest-5-ene in the presence of K-10 montmorillonite clay.     

Relation générale entre l'indice de liaison et la distance interatomique dans les molécules conjuguées,planes et linéaires

Two general relation between bond orderl and bond distance d (Å) are proposed:

1. between atomssp ₂-hybridised of second and third row: $$d_{PQ} = \left[ {0,731 + 0,3181\left( {n_P + n_Q } \right) - 0,1477\left( {\zeta _P + \zeta _Q } \right)} \right] - 0,020 + 0,0523\left( {\zeta _P + \zeta _Q } \right)l_{PQ} $$ ,ζ=Z/n,Z=Slater's effective nuclear charge of theπ-orbital).
2. between atomssp-hybridised of the second row: $$d_{PQ} = \left[ {1,904 - 0,123\left( {\zeta _P + \zeta _Q } \right)} \right] - \left[ {0,075 + 0,023\left( {\zeta _P + \zeta _Q } \right)} \right]l_{PQ} $$ (l=total bond orderπ+π′).

     

A Multicomponent Conjugation Strategy to Unique N‐Steroidal Peptides: First Evidence of the Steroidal Nucleus as a β‐Turn Inducer in Acyclic Peptides

Constraining small peptides into specific secondary structures has been a major challenge in peptide ligand design. So far, the major solution for decreasing the conformational flexibility in small peptides has been cyclization. An alternative is the use of topological templates, which are able to induce and/or stabilize peptide secondary structures by means of covalent attachment to the peptide. Herein a multicomponent strategy and structural analysis of a new type of peptidosteroid architecture having the steroid as N‐substituent of an internal amide bond is reported. The approach comprises the one‐pot conjugation of two peptide chains (or amino acid derivatives) to aminosteroids by means of the Ugi reaction to give a unique family of N‐steroidal peptides. The conjugation efficiency of a variety of peptide sequences and steroidal amines, as well as their consecutive head‐to‐tail cyclization to produce chimeric cyclopeptide–steroid conjugates, that is, macrocyclic lipopeptides, was assessed. Determination of the three‐dimensional structure of an acyclic N‐steroidal peptide in solution proved that the bulky, rigid steroidal template is capable of both increasing significantly the conformational rigidity, even in a peptide sequence as short as five amino acid residues, and inducing a β‐turn secondary structure even in the all‐s‐trans isomer. This report provides the first evidence of the steroid skeleton as β‐turn inducer in linear peptide sequences.     

Identification of uranyl binding proteins from human kidney-2 cell extracts by immobilized uranyl affinity chromatography and mass spectrometry

To improve our knowledge on protein targets of uranyl ion (UO₂²⁺), we set up a proteomic strategy based on immobilized metal-affinity chromatography (IMAC). The successful enrichment of UO₂²⁺-interacting proteins from human kidney-2 (HK-2) soluble cell extracts was obtained using an ion-exchange chromatography followed by a dedicated IMAC process previously described and designed for the uranyl ion. By mass spectrometry analysis we identified 64 proteins displaying varied functions. The use of a computational screening algorithm along with the particular ligand-based properties of the UO₂²⁺ ion allowed the analysis and categorization of the protein collection. This profitable approach demonstrated that most of these proteins fulfill criteria which could rationalize their binding to the UO₂²⁺-loaded phase. The obtained results enable us to focus on some targets for more in-depth studies and open new insights on its toxicity mechanisms at molecular level.