Structure Determination, Thermal Stability and Dissolution Rate of δ Indomethacin

<div> <p>The structure solution of the δ-polymorph of indomethacin was obtained using three-dimensional electron diffraction. This form shows a significantly enhanced dissolution rate compared with the more common and better studied α- and γ-polymorphs, indicating an increased bioavailability for medicinal applications. The structure was solved in non-centrosymmetric space group <i>P</i>2₁ and comprises two molecules in the asymmetric unit. Packing and molecule conformation closely resemble indomethacin methyl ester and indomethacin methanol solvate. Knowledge of the structure allowed the rational interpretation of spectroscopic IR and Raman data for δ-polymorph and a tentative interpretation for still unsolved indomethacin polymorphs. Finally, we observed a solid-solid transition from δ-polymorph to α-polymorph that can be driven by similarities in molecular conformation.</p> </div> <br>

Structure Determination, Thermal Stability and Dissolution Rate of δ Indomethacin

<div> <p>The structure solution of the δ-polymorph of indomethacin was obtained using three-dimensional electron diffraction. This form shows a significantly enhanced dissolution rate compared with the more common and better studied α- and γ-polymorphs, indicating an increased bioavailability for medicinal applications. The structure was solved in non-centrosymmetric space group <i>P</i>2₁ and comprises two molecules in the asymmetric unit. Packing and molecule conformation closely resemble indomethacin methyl ester and indomethacin methanol solvate. Knowledge of the structure allowed the rational interpretation of spectroscopic IR and Raman data for δ-polymorph and a tentative interpretation for still unsolved indomethacin polymorphs. Finally, we observed a solid-solid transition from δ-polymorph to α-polymorph that can be driven by similarities in molecular conformation.</p> </div> <br>

An X-shaped cyano–carbonyl interaction on the polar surface of (cyanoacetyl)hydrazones

An X-shaped CN⋯CO interaction, which plays a critical role in dictating the molecule conformation and crystal packing patterns, has been found to occur on the polar surface of (cyanoacetyl)hydrazones, and is rationalized by density functional theory calculations.

A single-molecule conformation modulating crystalline polymorph of a physical π–π pyrene dimer: blue and green emissions of a pyrene excimer

Blue fluorescence and green fluorescence were observed in two crystals with different pyrene dimers, which are modulated by the molecular conformation.

The Abnormal Oswald Ripening of Protein Nanofiber in Myofibrillar Protein Solution

In solutions of myofibrillar protein extracted from giant squid (Dosidicus gigas), the size-coarsening process of protein nanofiber is complex. At high temperature (25°C), nanofiber keeps growth but with two distinguishable patterns, slow rate at the initial stage with t0.2 and the fast one at the late stage with t2.3. The intersection of these two slopes is around 300 min. Meanwhile, protein concentration in solution enhances as well. These behaviors contradict to the prediction of Ostwald ripening. Thus, we call this process as abnormal. These abnormal behaviors come from the conformation change of some types of constitution protein molecules with chemical potential reduction when they dissolve from nanofiber to solution. On the other hand, low temperature (10°C) depresses this size growth. This observation suggests that temperature regulates protein molecule conformation change in nanofiber. The consequence of this abnormal Ostwald ripening process is that all protein molecules in nanofiber are redistributed. Protein molecules with the absence of conformation change in dissolution accumulate in nanofiber to cause it growing, while the rest concentrates in solution.

X-ray Structure Elucidation of a Pt-Metalloporphyrin and Its Application for Obtaining Sensitive AuNPs-Plasmonic Hybrids Capable of Detecting Triiodide Anions

The development of UV–vis spectrophotometric methods based on metalloporphyrins for fast, highly sensitive and selective anion detection, which avoids several of the practical challenges associated with other detection methods, is of tremendous importance in analytical chemistry. In this study, we focused on achieving a selective optical sensor for triiodide ion detection in traces based on a novel hybrid material comprised of Pt(II) 5,10,15,20-tetra(4-methoxy-phenyl)-porphyrin (PtTMeOPP) and gold nanoparticles (AuNPs). This sensor has high relevance in medical physiological tests. The structure of PtTMeOPP was investigated by single crystal X-ray diffraction in order to understand the metal surroundings and the molecule conformation and to assess if it qualifies as a potential sensitive material. It was proven that the Pt-porphyrin generated 1D H-bond supramolecular chains due to the weak C-H···O intermolecular hydrogen bonding. The presence of ordered voids in the crystal encouraged us to use PtTMeOPP as the sensing material for triiodide ion and to enhance its potential in a novel AuNPs/PtTMeOPP hybrid by the synergistic effects provided by the plasmonic gold nanoparticles. The spectrophotometric sensor is characterized by a detection limit of 1.5 × 10−9 M triiodide ion concentration and a remarkable confidence coefficient of 99.98%.

Influence of polyacrylamide conformation on fabric of “tunable” kaolin–polymer composite

“Tunable” clay–polymer composites have the potential to improve the engineering properties of clay materials. The importance of these materials derives from the ability of the responsive polymer to adopt various conformations (coiled, partially extended or extended), which in turn impacts the mesoscale properties of the material. However, the influence of polymer molecule conformation on particle arrangement and overall composite behavior is not well understood. The purpose of this study is to understand the fabric development due to the conformational behavior of the polymer, and thus the clay–polymer composite, over a wide range of solids content and stress levels. The polymer molecule conformation was controlled using selected fluid pH and ionic concentrations. Results show that the polymer conformation significantly influences clay fabric formation. When the polymer molecules are likely to have extended conformation, the dominant fabric mode is face-to-face and particle mobilization increases. Both face-to-face and edge-to-edge fabric formation dominate the behavior of the composite when coiled conformation is likely, resulting in a decrease in interparticle movement. Thus, the polymer conformation can be used to manipulate both the interparticle spacing between particles and (or) aggregates and arrangement of particles.

A Cautionary Tail: Changes in Integrin Behavior with Labeling

Genetic expression of fluorescently labeled proteins is essential to visualizing dynamic behavior within live cells. Recent advances in microscopy have increased resolution to the level where it is now possible to capture individual molecules interacting. However, the criteria for determining whether a fluorescent label perturbs protein function have not undergone a corresponding increase in resolution. The effects of protein labeling on cell function are still judged by whether populations of protein localize and interact with known binding partners. Here we use integrins, bidirectional signal adhesion molecules that regulate interactions between the extracellular matrix and the cytoskeleton through a well-defined series of conformational changes to show that not all labeling strategies are the same. We found that labeling the beta subunit decreased the mobility of individual integrin molecules and the protrusive activity of the entire cell. While integrins with labeled alpha subunits behaved similarly to unlabeled integrins, labeling the beta subunit increased the size of adhesions by elevating integrin affinity and exposing the ligand induced binding domain to change the molecule conformation. Thus, our single molecule and cellular data indicate that the ability of labeled proteins to localize and interact with known binding partners does not guarantee it does not alter protein function. We propose that the behaviors of individual molecules rather than the ensemble behavior of populations need to be considered as criteria to determine if a probe is non-perturbative.

Can we treat ab initio atomic charges and bond orders as conformation-independent electronic structure descriptors?

It is shown that atomic charges and bond orders of 2′-deoxycytidine depend on the molecule conformation.