Xylarkarynone A and B: Two Bioactive Eremophilane Sesquiterpenes from Xylaria sp. HHY-2.

A new compound xylarkarynone A (1), a first reported natural product compound xylarkarynone B (2) and eight known compounds (3-10) were isolated from Xylaria sp. HHY-2. Their structures were elucidated by spectroscopic methods, DP4+ probability analyses and electronic circular dichroism (ECD) calculations. The bioactivities of isolated compounds were assayed. Compound 1 exhibited obvious activity against A549 cells with an IC50 value of 6.12±0.28 µM. Additionally, compound 1 showed moderate antifungal activities against Plectosphaerella cucumerina and Aspergillus niger with minimum inhibitory concentrations (MICs) of both 16 µg/mL, which was at the same grade with positive control nystatin. Most compounds exhibited varying degrees of inhibitory activity against P. cucumerina, indicating that Xylaria sp. has potential as inhibitors against P. cucumerina.

Improved graph cut model with features of superpixels and neighborhood patches for myocardium segmentation from ultrasound image.

Ultrasound (US) imaging has the technical advantages for the functional evaluation of myocardium compared with other imaging modalities. However, it is a challenge of extracting the myocardial tissues from the background due to low quality of US imaging. To better extract the myocardial tissues, this study proposes a semi-supervised segmentation method of fast Superpixels and Neighborhood Patches based Continuous Min-Cut (fSP-CMC). The US image is represented by a graph, which is constructed depending on the features of superpixels and neighborhood patches. A novel similarity measure is defined to capture and enhance the features correlation using Pearson correlation coefficient and Pearson distance. Interactive labels provided by user play a subsidiary role in the semi-supervised segmentation. The continuous graph cut model is solved via a fast minimization algorithm based on augmented Lagrangian and operator splitting. Additionally, Non-Uniform Rational B-Spline (NURBS) curve fitting is used as post-processing to solve the low resolution problem caused by the graph-based method. 200 B-mode US images of left ventricle of the rats were collected in this study. The myocardial tissues were segmented using the proposed fSP-CMC method compared with the method of fast Neighborhood Patches based Continuous Min-Cut (fP-CMC). The results show that the fSP-CMC segmented the myocardial tissues with a higher agreement with the ground truth (GT) provided by medical experts. The mean absolute distance (MAD) and Hausdorff distance (HD) were significantly lower than those values of fP-CMC (p < 0.05), while the Dice was significantly higher (p < 0.05). In conclusion, the proposed fSP-CMC method accurately and effectively segments the myocardiumn in US images. This method has potentials to be a reliable segmentation method and useful for the functional evaluation of myocardium in the future study.

Global Tracking of Myocardial Motion in Ultrasound Sequence Images: A Feasibility Study.

The assessment of myocardial motion plays a promising role in the evaluation of cardiac function. This study aims to propose a novel framework of global estimation of the myocardial motion using radio-frequency (RF) data. The framework consists of B-mode image reconstruction, displacement estimation, myocardium extraction, and image fusion. The RF data of murine heart in parasternal long-axis (PLAX) view were collected for B-mode image reconstruction and displacement estimation. The vectorized normalized cross-correlation (VNCC) approach was proposed to globally estimate the displacements of the RF frames, while a sum-table based normalized cross-correlation (STNCC) was performed as reference algorithm. The bimodal fusion images were obtained to visualize the motion and anatomical structure of myocardium by an improved fast mapping algorithm (IFMA). In comparison with STNCC, the computation time of displacement using VNCC reduced by approximate 10s. The myocardial motions of anterior wall and posterior wall during one cardiac cycle were similarly tracked by VNCC as that of STNCC. The averaged absolute error in displacement between the two methods ranges from 1 to 3µm. The obtained myocardial elastographic images using VNCC intuitively present the morphological and mechanical changes during the contraction period of left ventricle. The results demonstrate that the proposed framework is an efficient tool for the estimation of myocardial motion reflecting cardiac systolic function. This approach has potentials to provide visualized information of myocardium for diagnosis and prognosis of cardiovascular diseases (CVDs).

Conjugates of poly(DL-lactide-co-glycolide) on amino cyclodextrins and their nanoparticles as protein delivery system.

Poly(DL-lactide-co-glycolide) (PLG) was chemically conjugated on two amino cyclodextrins, mono(6-(2-aminoethyl)amino-6-deoxy)-beta-cyclodextrin and ethylenediamino bridged bis(beta-cyclodextrin), to afford novel amphiphilic conjugates. Those conjugates were then characterized with infrared spectrometry (IR), proton nuclear magnetic resonance ((1)H NMR) and gel permeation chromatography (GPC). A repeat-nanoprecipitation (RP-NP) method was also developed to fabricate the nanoparticles of the conjugates with a water-soluble model protein, bovine serum albumin (BSA). At the end of RP-NP process, the availability of BSA was over 80% while the entrapment efficiency was 40-50% for each nanoprecipitation. The nanoparticles were rigid and spherical with diameters of 110-180 nm determined by transmission electron microscope (TEM), atomic force microscopy (AFM) and particle size analyzer. Nanoparticles possessed good steric stability during freeze-drying and resuspensions due to the existence of cyclodextrins corona. Interactions between BSA and the conjugates in the nanoparticles were then elucidated with IR experiments. About 25% BSA adsorbed on the surface of nanoparticles due to the interaction and was easy to release in the first day. The release of BSA from the nanoparticles was in three phases: a burst effect in the first day, a followed plateau in about a week, and a sustained release of the protein over 14 days. By changing the lactide/glycolide ratio, the degradation time of the conjugates and the release rate of BSA could be controlled. The loss of CDs content was faster than that of overall Mw during degradation since CDs formed outer corona of the nanoparticles. Both the novel biomaterials and the nanosphere fabrication technique contributed to the maintenance of protein structure.

Aggregation of two carboxylic derivatives of porphyrin and their affinity to bovine serum albumin.

Aggregation of two porphyrin derivatives with carboxylic groups, 4-oxo-4-((4-(10,15,20-triphenyl-21H,23H-porphin-5-yl)phenyl)amino)butanoic acid (MAC) and 4,4',4'',4'''-[21H,23H-porphine-5,10,15,20-tetrayltetrakis(4,1-phenyleneimino)]tetrakis(4-oxo-butanoic acid) (TA4C), and their affinity to bovine serum albumin were investigated via absorption spectrometry, (1)H NMR and fluorescence spectrometry. MAC and its complexes with beta-cyclodextrin could form aggregates in an aqueous solution while TA4C was self-associated loosely. From the absorbance profiles of MAC in the titration of bovine serum albumin, hypochromicity was observed without any shift of the maximum absorbance wavelength. In both absorption spectra of TA4C in aqueous solutions and in solid state, three Q bands appeared in the visible region. In the measurements of absorption and fluorescence spectra upon titration of BSA, some spectral changes of TA4C were observed. The whole procedure of titration could be divided into three successive stages. The three-banded profiles of TA4C might be explained according to a loose dimer model.

Interactions of some modified mono- and bis-beta-cyclodextrins with bovine serum albumin.

Two mono-substituted beta-cyclodextrins and two bridged bis-beta-cyclodextrins, that is, mono(6-(2-aminoethylamino)-6-deoxy)-beta-cyclodextrin (1), mono(6-(2-(2-aminoethylamino)ethylamino)-6-deoxy)-beta-cyclodextrin (2), ethylene-1,2-diamino bis-6-(6-deoxy-beta-cyclodextrin) (3), and iminodiethylene-2,2'-diamino bis-6-(6-deoxy-beta-cyclodextrin) (4), were prepared from beta-cyclodextrin. Their binding ability with bovine serum albumin as a model protein was investigated through proton magnetic resonance (1H NMR), ultraviolet visible spectroscopy (UV-vis), circular dichroism (CD), and fluorescence spectroscopy. In the 1H NMR spectra of the modified cyclodextrins, the resolution of proton signals decreases after the addition of BSA. From the UV and CD spectra, it is found that both the UV absorption and the alpha-helix content of BSA increase with the concentration of the modified cyclodextrins. The protein-ligand interactions cause a fluorescence quenching. The quenching constants are determined using the Stern-Volmer equation to provide an observation of the binding affinity between modified cyclodextrins and BSA. All these results indicate that the modified cyclodextrins can interact with BSA and the bridged bis(beta-cyclodextrin)s (3 and 4) have much stronger interactions than the mono-substituted beta-cyclodextrins (1 and 2). The strong binding stability of bis-cyclodextrins should be attributed to the cooperative effect of two adjacent cyclodextrin moieties. Job's plot shows that the complex stoichiometries of BSA to the modified cyclodextrins were 1:4 for 1 and 2, as well as 1:3 for 3 and 4, respectively.