22 research outputs found
Are the Follicular Fluid Characteristics of Recovered Coronavirus Disease 2019 Patients Different From Those of Vaccinated Women Approaching in vitro Fertilization?
The aim of this pilot study is to evaluate if SARS-CoV-2 infection or vaccination against SARS-CoV-2 infection induce observable metabolic effects in follicular fluid of women who are following in vitro fertilization (IVF) treatments. The possible impact of coronavirus disease 2019 (COVID-19) on fertility and IVF outcome is considered. We have selected for this study: six women vaccinated against SARS-CoV-2 infection, five recovered COVID-19 patients, and we used nine healthy women as the control group. At the time of oocytes retrieval from participants in the study, follicular fluids were collected and metabolomic analysis was performed by 1H NMR spectroscopy in combination with multivariate analysis to interpret the spectral data. The search for antibody positivity in the follicular fluid aspirates was also carried out, together with the western blotting analysis of some inflammatory proteins, interleukin-6, tumor necrosis factor α (TNFα), and the free radical scavenger superoxide dismutase 2. Higher levels of Ala and Pro together with lower levels of lipids and trimethylamine N-oxide (TMAO) were found in follicular fluids (FFs) of vaccinated women while lower levels of many metabolites were detected in FFs of recovered COVID patients. Expression level of TNF-α was significantly lower both in recovered COVID-19 patients and vaccinated women in comparison to healthy controls
Structural characterization of the transmembrane segments of the mitochondrial oxoglutarate carrier (OGC)by NMR spectroscopy
Abstract. The oxoglutarate carrier (OGC) is a member of the mitochondrial carrier protein superfamily, which
includes the ADP/ATP carrier and other functionally characterized members, and exchanges cytosolic malate
for 2-oxoglutarate from the mitochondrial matrix. By means of CD and NMR spectroscopy, we previously
characterized four synthetic peptides containing transmembrane segments (TMSs) I, II, V and VI of the OGC,
respectively, in TFE/water mixtures and SDS micelles. Here, we present data on the remaining
transmembrane segments of OGC obtained by performing CD and NMR studies on peptides corresponding
to TMS-III and TMS-IV. In TFE/water, alpha-helical structures were found for these peptides in the L121-R146 and
T187-S201 regions, respectively. We also evaluated the compatibility between the helical structures of our
peptides and a homology model of the OGC based on the available X-ray structure of the ATP/ADP carrier.
Key words: NMR; mitochondrial carriers; mitochondrial oxoglutarate carrier; structure; transmembrane segments
NMR, molecular mechanism and molecular dynamics study of Proctolin (RYLPT-OH): an insect neuropeptide.
Effect of some cellular metabolic intermediates on the mitochondrial carrier expression.
NMR studies of a series of dehydrodermorphins
The third and fifth aromatic residues of dermorphin, a potent mu-opioid peptide, and of its N-terminal fragments, from the pentapeptide to the parent heptapeptide amide, have been systematically substituted with Z-dehydrophenylalanine (delta-Phe) and/or Phe to investigate the conformation-activity relationship. The characterization in DMSO-d6 at 500 MHz indicates that, in this solvent, all peptides adopt essentially random, extended conformations, as a consequence of the strong solvation. The chemical shift of the methyl group of D-Ala is influenced by the precise orientation of the side chain of the third residue in a fashion that can be correlated to the mu potency, consistently with our model of mu-receptor. However, the complexes of the pentapeptides with 18-crown-6-ether, when dissolved in chloroform, adopt ordered, folded conformations, a behavior that closely parallels the CD observations in methanol
QUALITY CONTROL OF THE CURE PROCESS OF THERMOSETTING RESINS BY MEANS OF DIFFERENTIAL SCANNING CALORIMETRY
Structure-activity relatioships of tetrapeptides related to dermorphin: a 500-MHz 1H-nmr study
Several tetrapeptide analogs of dermorphin have been studied by means of 1H-nmr spectroscopy at 500 MHz in DMSO-d6. In spite of the unfavorable properties of the solvent, it is possible to extract key structural information that, combined with the biological activity of the peptides, yields a structure–activity relationship that is consistent with our model of the μ receptor site. In particular, the importance of the orientation of the aromatic ring of the third residue, hypothesized in the theoretical model, is now substantiated. The shape of the P subsite of the receptor is also indirectly defined by the shape of several bulky side chains of the third residue