Green Process to Prepare Silk Fibroin/Gelatin Biomaterial Scaffolds

A new all‐aqueous and green process is described to form three‐dimensional porous silk fibroin matrices with control of structural and morphological features. Silk‐based scaffolds are prepared using lyophilization. Gelatin is added to the aqueous silk fibroin solution to change the silk fibroin conformation and silk fibroin–water interactions through adjusting the hydrophilic interactions in silk fibroin–gelatin–water systems to restrain the formation of separate sheet like structures in the material, resulting in a more homogenous structure. Water annealing is used to generate insolubility in the silk fibroin–gelatin scaffold system, thereby avoiding the use of organic solvents such as methanol to lock in the β‐sheet structure. The adjusting of the concentration of gelatin, as well as the concentration of silk fibroin, leads to control of morphological and functional properties of the scaffolds. The scaffolds were homogeneous in terms of interconnected pores, with pore sizes ranging from 100 to 600 µm, depending on the concentration of silk fibroin used in the process. At the same time, the morphology of the scaffolds changed from lamellar sheets to porous structures based on the increase in gelatin content. Compared with salt‐leaching aqueous‐derived scaffolds and hexafluoroisopropanol (HFIP)‐derived scaffolds, these freeze‐dried scaffolds had a lower content of β‐sheet, resulting in more hydrophilic features. Most of gelatin was entrapped in the silk fibroin–gelatin scaffolds, without the burst release in PBS solution. During in vitro cell culture, these silk fibroin–gelatin scaffolds had improved cell‐compatibility than salt‐leaching silk fibroin scaffolds. This new process provides useful silk fibroin‐based scaffold systems for use in tissue engineering. Furthermore, the whole process is green, including all‐aqueous, room temperature and pressure, and without the use of toxic chemicals or solvents, offering new ways to load bioactive drugs or growth factors into the process.

     

Role of Polyalanine Domains in β‐Sheet Formation in Spider Silk Block Copolymers

Genetically engineered spider silk‐like block copolymers were studied to determine the influence of polyalanine domain size on secondary structure. The role of polyalanine block distribution on β‐sheet formation was explored using FT‐IR and WAXS. The number of polyalanine blocks had a direct effect on the formation of crystalline β‐sheets, reflected in the change in crystallinity index as the blocks of polyalanines increased. WAXS analysis confirmed the crystalline nature of the sample with the largest number of polyalanine blocks. This approach provides a platform for further exploration of the role of specific amino acid chemistries in regulating the assembly of β‐sheet secondary structures, leading to options to regulate material properties through manipulation of this key component in spider silks.

     

Peculiarities of grid control over the current in a discharge with a cathode spot on the cesium liquid-metal cathode

We report on the results of successful implementation of full grid control in a cesium discharge with a cathode spot. The discharge is quenched by a negative grid pulse for a discharge current density up to 75 A/cm² in the grid plane for voltage switching up to 100 V in the pressure range 0.5–1.5 Pa for a voltage drop of 5–6 V in the discharge. It is shown that quenching is the break-off type. The discovered effect of “evacuation” of the heavy component (ions) from the grid-anode gap to the cathode region leads to an unusually long (hundreds of microseconds) time of stabilization of the steady state in the discharge under the experimental conditions.     

A New Algorithm for Solving the Word Problem in Braid Groups

One of the most interesting questions about a group is whether its word problem can be solved and how. The word problem in the braid group is of particular interest to topologists, algebraists, and geometers, and is the target of intensive current research. We look at the braid group from a topological point of view (rather than a geometric one). The braid group is defined by the action of diffeomorphisms on the fundamental group of a punctured disk. We exploit the topological definition in order to give a new approach for solving its word problem. Our algorithm, although not better in complexity, is faster in comparison with known algorithms for short braid words, and it is almost independent of the number of strings in the braids. Moreover, the algorithm is based on a new computer presentation of the elements of the fundamental group of a punctured disk. This presentation can be used also for other algorithms.     

μ+SR frequency shifts in the van‐Vleck paramagnet PrIn3

As part of an ongoing μ⁺SR study on cubic van‐Vleck paramagnets of the PrM₃ series ( M\ =\ In,Pb,Tl,Sn), in which the CEF level scheme varies systematically, we present preliminary static μ⁺SR results on a single crystal of PrIn₃. From the angular dependence and from the appearance of the μSR spectra, we could determine that stopped μ⁺ occupy octahedral sites of the (1/2, 0, 0) type, i.e. sites with 2 Pr and 4 In atoms as neighbors. The spectral frequency shifts can be accounted for by assigning to the Pr sites essentially unperturbed 4f dipole moment values, as derived from bulk magnetization measurements. The temperature dependence of the shifts scales to a good accuracy with the bulk susceptibility. It is concluded that unlike previous observations with PrNi₅, the local perturbations induced by an interstitial μ⁺ on the CEF levels of neighboring Pr in the PrIn₃ system are small compared with the unperturbed level splitting itself. This revised version was published online in July 2006 with corrections to the Cover Date.     

An Efficient Labelling Approach to Harness Backbone and Side‐Chain Protons in 1H‐Detected Solid‐State NMR Spectroscopy

¹H‐detection can greatly improve spectral sensitivity in biological solid‐state NMR (ssNMR), thus allowing the study of larger and more complex proteins. However, the general requirement to perdeuterate proteins critically curtails the potential of ¹H‐detection by the loss of aliphatic side‐chain protons, which are important probes for protein structure and function. Introduced herein is a labelling scheme for ¹H‐detected ssNMR, and it gives high quality spectra for both side‐chain and backbone protons, and allows quantitative assignments and aids in probing interresidual contacts. Excellent ¹H resolution in membrane proteins is obtained, the topology and dynamics of an ion channel were studied. This labelling scheme will open new avenues for the study of challenging proteins by ssNMR.