Cd Conformational And Modeling Studies Of A Synthetic Peptide Vpdlladllk In Different Media

CD spectral studies of VPDLLADLK, a synthetic peptide shows that it undergoes a conformational transition from an unordered structure to a more ordered structure from a polar to a non-polar homogeneous medium. In microheterogeneous media like SDS, CTAB micelles and DMPC lipid bilayer, the peptide exhibits a more stable alpha- helical structure. The helical conformation is stabilized in DMPC lipid bilayer. Homology modeling gives the picture of alpha- helix, where the middle six residues LLADLL form the turns of the helix

Conformation of gramicidin-A in CTAB micellar media

Gramicidin A (gA) is a linear pentadecapeptide, which exhibits various conformations depending on the environment. The conformational behavior of gA in spherical and rod-shaped cationic micelles formed by cetyltrimethylammonium bromide (CTAB) surfactant has been studied using circular dichroism (CD) and fluorescence spectroscopy, and a probable structure of gramicidin A in CTAB media has been proposed. A CD study shows that gramicidin A assumes$\beta^{ 6.3}$ helical structure in cationic spherical as well as rod-shaped CTAB micellar media. Modeling studies show the flexibility of the side chain conformation particularly in tryptophan-9. Study of intrinsic fluorescence of tryptophans in gramicidin A indicates three distinct environments for the four-tryptopha

Conformation of gramicidin-A in CTAB micellar media

Gramicidin A (gA) is a linear pentadecapeptide, which exhibits various conformations depending on the environment. The conformational behavior of gA in spherical and rod-shaped cationic micelles formed by cetyltrimethylammonium bromide (CTAB) surfactant has been studied using circular dichroism (CD) and fluorescence spectroscopy, and a probable structure of gramicidin A in CTAB media has been proposed. A CD study shows that gramicidin A assumes β6.3 helical structure in cationic spherical as well as rod-shaped CTAB micellar media. Modeling studies show the flexibility of the side chain conformation particularly in tryptophan-9. Study of intrinsic fluorescence of tryptophans in gramicidin A indicates three distinct environments for the four-tryptophan residues in CTAB media

Visuo-spatial construction in patients with frontal and parietal lobe lesions

Visuospatial construction, traditionally viewed as a putative parietal function, also requires sustained attention, planning, organization strategies and error correction, and hence frontal lobe mediation. The relative contributions of the frontal and parietal lobes are poorly understood. To examine the contributions of parietal, frontal lobes, as well as right and left cerebral hemispheres to visuospatial construction. The Stick Construction Test for two-dimensional construction and the Block Construction Test for three-dimensional construction were administered pre-surgically to patients with lesions in the parietal lobe (n =9) and the frontal lobe (n=11), along with normal control subjects (n =20) matched to the patients on age (+/- 3 years), gender, education (+/- 3 years) and handedness. The patients were significantly slower than the controls on both two-dimensional and three-dimensional tests. Patients with parietal lesions were slower than those with frontal lesions on the test of three-dimensional construction. Within each lobe patients with right and left sided lesions did not differ significantly. It appears that tests of three-dimensional construction might be most sensitive to visuospatial construction deficits. Visuospatial construction involves the mediation of both frontal and parietal lobes. The function does not appear to be lateralized. The networks arising from the parieto-occipital areas and projecting to the frontal cortices (e.g., occipito-frontal fasciculus) may be the basis of the mediation of both lobes in visuospatial construction. The present findings need replication from studies with larger sample sizes

Effects of Disease-Causing Mutations on the Conformation of Human Apolipoprotein A‑I in Model Lipoproteins

Plasma high-density lipoproteins (HDLs) are protein–lipid nanoparticles that transport lipids and protect against atherosclerosis. Human apolipoprotein A-I (apoA-I) is the principal HDL protein whose mutations can cause either aberrant lipid metabolism or amyloid disease. Hydrogen–deuterium exchange (HDX) mass spectrometry (MS) was used to study the apoA-I conformation in model discoidal lipoproteins similar in size to large plasma HDL. We examined how point mutations associated with hereditary amyloidosis (F71Y and L170P) or atherosclerosis (L159R) influence the local apoA-I conformation in model lipoproteins. Unlike other apoA-I forms, the large particles showed minimal conformational heterogeneity, suggesting a fully extended protein conformation. Mutation-induced structural perturbations in lipid-bound protein were attenuated compared to the free protein and indicated close coupling between the two belt-forming apoA-I molecules. These perturbations propagated to distant lipoprotein sites, either increasing or decreasing their protection. This HDX MS study of large model HDL, compared with previous studies of smaller particles, ascertained that apoA-I’s central region helps accommodate the protein conformation to lipoproteins of various sizes. This study also reveals that the effects of mutations on lipoprotein conformational dynamics are much weaker than those in a lipid-free protein. Interestingly, the mutation-induced perturbations propagate to distant sites nearly 10 nm away and alter their protection in ways that cannot be predicted from the lipoprotein structure and stability. We propose that long-range mutational effects are mediated by both protein and lipid and can influence lipoprotein functionality

Seasonal clustering of sinopulmonary mucormycosis in patients with hematologic malignancies at a large comprehensive cancer center

Abstract Background Invasive Mucorales infections (IMI) lead to significant morbidity and mortality in immunocompromised hosts. The role of season and climatic conditions in case clustering of IMI remain poorly understood. Methods Following detection of a cluster of sinopulmonary IMIs in patients with hematologic malignancies, we reviewed center-based medical records of all patients with IMIs and other invasive fungal infections (IFIs) between January of 2012 and August of 2015 to assess for case clustering in relation to seasonality. Results A cluster of 7 patients were identified with sinopulmonary IMIs (Rhizopus microsporus/azygosporus, 6; Rhizomucor pusillus, 1) during a 3 month period between June and August of 2014. All patients died or were discharged to hospice. The cluster was managed with institution of standardized posaconazole prophylaxis to high-risk patients and patient use of N-95 masks when outside of protected areas on the inpatient service. Review of an earlier study period identified 11 patients with IMIs of varying species over the preceding 29 months without evidence of clustering. There were 9 total IMIs in the later study period (12 month post-initial cluster) with 5 additional cases in the summer months, again suggesting seasonal clustering. Extensive environmental sampling did not reveal a source of mold. Using local climatological data abstracted from National Centers for Environmental Information the clusters appeared to be associated with high temperatures and low precipitation. Conclusions Sinopulmonary Mucorales clusters at our center had a seasonal variation which appeared to be related to temperature and precipitation. Given the significant mortality associated with IMIs, local climatic conditions may need to be considered when considering center specific fungal prevention and prophylaxis strategies for high-risk patients