Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Sugar-derived oxazolone pseudotetrapeptide as ?-turn inducer and anion-selective transporter.

ABSTRACT: The intramolecular cyclization of a C-3-tetrasubstituted furanoid sugar amino acid-derived linear tetrapeptide afforded an oxazolone pseudo-peptide with the formation of an oxazole ring at the C-terminus. A conformational study of the oxazolone pseudo-peptide showed intramolecular C=O···HN(II) hydrogen bonding in a seven-membered ring leading to a ?-turn conformation. This fact was supported by a solution-state NMR and molecular modeling studies. The oxazolone pseudotetrapeptide was found to be a better Cl--selective transporter for which an anion-anion antiport mechanism was established.

SUBMITTER: Burade SS

PROVIDER: S-EPMC6808195 | biostudies-literature | 2019

REPOSITORIES: biostudies-literature

ACCESS DATA

Json Xml

Publications

Sugar-derived oxazolone pseudotetrapeptide as γ-turn inducer and anion-selective transporter.

Burade Sachin S SS Pawar Sushil V SV Saha Tanmoy T Kumbhar Navanath N Kotmale Amol S AS Ahmad Manzoor M Talukdar Pinaki P Dhavale Dilip D DD

Beilstein journal of organic chemistry 20191014

The intramolecular cyclization of a C-3-tetrasubstituted furanoid sugar amino acid-derived linear tetrapeptide afforded an oxazolone pseudo-peptide with the formation of an oxazole ring at the <i>C</i>-terminus. A conformational study of the oxazolone pseudo-peptide showed intramolecular C=O···HN(II) hydrogen bonding in a seven-membered ring leading to a γ-turn conformation. This fact was supported by a solution-state NMR and molecular modeling studies. The oxazolone pseudotetrapeptide was found ...[more]

PMID: 31666876

Similar Datasets

Novel acridine-based thiosemicarbazones as 'turn-on' chemosensors for selective recognition of fluoride anion: a spectroscopic and theoretical study.

Project description:New thiosemicarbazide-linked acridines 3a-c were prepared and investigated as chemosensors for the detection of biologically and environmentally important anions. The compounds 3a-c were found selective for fluoride (F-) with no affinity for other anions, i.e. -OAc, Br-, I-, HSO4-, SO42-, PO43-, ClO3-, ClO4-, CN- and SCN-. Further, upon the gradual addition of a fluoride anion (F-) source (tetrabutylammonium fluoride), a well-defined change in colour of the solution of probes 3a-c was observed. The anion-sensing process was studied in detail via UV-visible absorption, fluorescence and 1H-NMR experiments. Moreover, during the synthesis of acridine probes 3a-c nickel fluoride (NiF2), a rarely explored transition metal fluoride salt, was used as the catalyst. Theoretical studies via density functional theory were also carried out to further investigate the sensing and anion (F-) selectivity pattern of these probes.

| S-EPMC6083729 | biostudies-literature

Cellular metabolic activity marker via selective turn-ON detection of transporter protein using nitrobenzoxadiazole-based fluorescent reporter.

Project description:A nitrobenzoxadiazole-based fluoroprobe (NBD-Bu) is designed to probe cellular metabolic activity in cancer and normal cells. NBD-Bu shows a significant fluorescence enhancement upon selective binding to the transport protein serum albumin in PBS buffer at ambient conditions. Encouraged by this finding, the site- specificity of NBD-Bu has been explored through a competitive displacement assay in the presence of site-specific markers such as warfarin and ibuprofen. Notably, even at micromolar concentrations, the probe possesses the ability to displace the site marker drug ibuprofen, efficiently. Subsequently, high-resolution fluorescence imaging results consolidated the potential of NBD-Bu for detection of abnormal cellular metabolic activity.

| S-EPMC7058046 | biostudies-literature

Organic anion transporter 2 (SLC22A7) is a facilitative transporter of cGMP.

Project description:The second messenger, cGMP, mediates a host of cellular responses to various stimuli, resulting in the regulation of many critical physiologic functions. The existence of specific cGMP transporters on the plasma membrane that participate in the regulation of cGMP levels has been suggested in a large number of studies. In this study, we identified a novel plasma membrane transporter for cGMP. In particular, we showed that hOAT2 (SLC22A7), a member of the solute carrier (SLC) superfamily, was a facilitative transporter for cGMP and other guanine nucleotides. hOAT2, which is ubiquitously expressed at high levels in many cell types, was previously thought to primarily transport organic anions. Among purine and pyrimidine nucleobases, nucleosides, and nucleotides, hOAT2 showed the greatest preference for cGMP, which transported cGMP with a K(m) value of 88 +/- 11 muM and exhibited between 50- and 100-fold enhanced uptake over control cells. Our data revealed that hOAT2 is a bidirectional facilitative transporter that can control both intracellular and extracellular levels of cGMP. In addition, we observed that a common alternatively spliced variant of hOAT2 demonstrated a complete loss of transport function as a result of a low expression level on the plasma membrane. We conclude that hOAT2 is a highly efficient, facilitative transporter of cGMP and may be involved in cGMP signaling in many tissues. Our study suggests that hOAT2 represents a potential new drug target for regulating cGMP levels.

| S-EPMC2698938 | biostudies-literature

A common inducer molecule enhances sugar utilization by Shewanella oneidensis MR-1.

Project description:Shewanella oneidensis MR-1 is an electroactive bacterium that is a promising host for bioelectrochemical technologies, which makes it a common target for genetic engineering, including gene deletions and expression of heterologous pathways. Expression of heterologous genes and gene knockdown via CRISPRi in S. oneidensis are both frequently induced by β-D-1-thiogalactopyranoside (IPTG), a commonly used inducer molecule across many model organisms. Here, we report and characterize an unexpected phenotype; IPTG enhances the growth of wild-type S. oneidensis MR-1 on the sugar substrate N-acetylglucosamine (NAG). IPTG improves the carrying capacity of S. oneidensis growing on NAG while the growth rate remains similar to cultures without the inducer. Extracellular acetate accumulates faster and to a higher concentration in cultures without IPTG than those with it. IPTG appears to improve acetate metabolism, which combats the negative effect that acetate accumulation has on the growth of S. oneidensis with NAG. We recommend using extensive experimental controls and careful data interpretation when using both NAG and IPTG in S. oneidensis cultures.

| S-EPMC10549210 | biostudies-literature

Review of Transporter Substrate, Inhibitor, and Inducer Characteristics of Cladribine.

Project description:Cladribine is a nucleoside analog that is phosphorylated in its target cells (B- and T-lymphocytes) to its active adenosine triphosphate form (2-chlorodeoxyadenosine triphosphate). Cladribine tablets 10 mg (Mavenclad®) administered for up to 10 days per year in 2 consecutive years (3.5-mg/kg cumulative dose over 2 years) are used to treat patients with relapsing multiple sclerosis. The ATP-binding cassette, solute carrier, and nucleoside transporter substrate, inhibitor, and inducer characteristics of cladribine are reviewed in this article. Available evidence suggests that the distribution of cladribine across biological membranes is facilitated by a number of uptake and efflux transporters. Among the key ATP-binding cassette efflux transporters, only breast cancer resistance protein has been shown to be an efficient transporter of cladribine, while P-glycoprotein does not transport cladribine well. Intestinal absorption, distribution throughout the body, and intracellular uptake of cladribine appear to be exclusively mediated by equilibrative and concentrative nucleoside transporters, specifically by ENT1, ENT2, ENT4, CNT2 (low affinity), and CNT3. Renal excretion of cladribine appears to be most likely driven by breast cancer resistance protein, ENT1, and P-glycoprotein. The latter may play a role despite its poor cladribine transport efficiency in view of the renal abundance of P-glycoprotein. There is no evidence that solute carrier uptake transporters such as organic anion transporting polypeptides, organic anion transporters, and organic cation transporters are involved in the transport of cladribine. Available in vitro studies examining the inhibitor characteristics of cladribine for a total of 13 major ATP-binding cassette, solute carrier, and CNT transporters indicate that in vivo inhibition of any of these transporters by cladribine is unlikely.

| S-EPMC8613159 | biostudies-literature

Anion- and proton-dependent gating of ClC-4 anion/proton transporter under uncoupling conditions.

Project description:ClC-4 is a secondary active transporter that exchanges Cl(-) ions and H(+) with a 2:1 stoichiometry. In external SCN(-), ClC-4 becomes uncoupled and transports anions with high unitary transport rate. Upon voltage steps, the number of active transporters varies in a time-dependent manner, resembling voltage-dependent gating of ion channels. We here investigated modification of the voltage dependence of uncoupled ClC-4 by protons and anions to quantify association of substrates with the transporter. External acidification shifts voltage dependence of ClC-4 transport to more positive potentials and leads to reduced transport currents. Internal pH changes had less pronounced effects. Uncoupled ClC-4 transport is facilitated by elevated external [SCN(-)] but impaired by internal Cl(-) and I(-). Block by internal anions indicates the existence of an internal anion-binding site with high affinity that is not present in ClC channels. The voltage dependence of ClC-4 coupled transport is modulated by external protons and internal Cl(-) in a manner similar to what is observed under uncoupling conditions. Our data illustrate functional differences but also similarities between ClC channels and transporters.

| S-EPMC3043216 | biostudies-literature

Kidney-specific Dysfunction of the Organic Anion Transporter MRP2 (ABCC2): Functional Consequences for Renal Grafts

Project description:Transplanting renal allografts represents the major curative treatment of chronic renal failure. Despite recent advances in immunosuppressive therapy, long-term survival of allografts remains a major clinical problem. Kidney function depends in part on transport proteins such as MRP2 (ABCC2) which facilitates renal secretion of amphiphilic exogenous and endogenous compounds. Inherited variants of genes not related to the immune system have been shown to modify the outcome after renal transplantation. We investigated whether ABCC2 gene variants in the donor kidney affect renal graft function. A congenic rat model was established carrying a single nucleotide deletion in the ABCC2 gene. Renal cross transplantations were performed with wild type rats. Renal excretion of the MRP2 substrates bilirubin glucuronide and p-aminohippuric acid, but not morphine-6-glucuronide, was affected by the donor genotype. Moreover, proteomic analyses and transcriptional profiling revealed modified expression patterns indicative of increased oxidative stress in renal grafts carrying the mutated gene. In the clinical part our study, we assessed ABCC2 haplotypes in renal transplant patients and evaluated graft function. The 3563T>A gene polymorphism was significantly associated with delayed graft function. Together, both experimental and clinical data show that the ABCC2 genotype of the donor kidney affects renal graft function. Keywords: dysfunction of organic anion transporter MRP2 (ABCC2)

2009-08-27 | GSE10949 | GEO

A Loose Relationship: Incomplete H+/Sugar Coupling in the MFS Sugar Transporter GlcP.

Project description:The glucose transporter from Staphylococcus epidermidis, GlcPSe, is a homolog of the human GLUT sugar transporters of the major facilitator superfamily. Together with the xylose transporter from Escherichia coli, XylEEc, the other prominent prokaryotic GLUT homolog, GlcPSe, is equipped with a conserved proton-binding site arguing for an electrogenic transport mode. However, the electrophysiological analysis of GlcPSe presented here reveals important differences between the two GLUT homologs. GlcPSe, unlike XylEEc, does not perform steady-state electrogenic transport at symmetrical pH conditions. Furthermore, when a pH gradient is applied, partially uncoupled transport modes can be generated. In contrast to other bacterial sugar transporters analyzed so far, in GlcPSe sugar binding, translocation and release are also accomplished by the deprotonated transporter. Based on these experimental results, we conclude that coupling of sugar and H+ transport is incomplete in GlcPSe. To verify the viability of the observed partially coupled GlcPSe transport modes, we propose a universal eight-state kinetic model in which any degree of coupling is realized and H+/sugar symport represents only a specific instance. Furthermore, using sequence comparison with strictly coupled XylEEc and similar sugar transporters, we identify an additional charged residue that may be essential for effective H+/sugar symport.

| S-EPMC5770559 | biostudies-literature

Overexpression of the tonoplast sugar transporter CmTST2 in melon fruit increases sugar accumulation.

Project description:Fruits are an important part of the human diet and sugar content is a major criterion used to evaluate fruit quality. Melon fruit accumulate high sugar concentrations during their development; however, the mechanism through which these sugars are transported into the vacuoles of fruit cells for storage remains unclear. In this study, three tonoplast sugar transporters (TSTs), CmTST1, CmTST2, and CmTST3, were isolated from melon plants. Analysis of subcellular localization revealed that all these proteins were targeted to the tonoplast, and evaluation of spatial expression and promoter-GUS activity indicated that they had different expression patterns in the plant. RT-PCR and qRT-PCR results indicated that CmTST2 exhibited the highest expression level among the TST isoforms during melon fruit development. Histochemical and immunohistochemistry localization experiments were performed to identify the tissue- and cell-type localization of CmTST2 in the fruit, and the results indicated that both its transcription and translation were in the mesocarp and vascular cells. Overexpressing the CmTST2 gene in strawberry fruit and cucumber plants by transient expression and stable transformation, respectively, both increased sucrose, fructose, and glucose accumulation in the fruit. The results indicate that CmTST2 plays an important role in sugar accumulation in melon fruit.

| S-EPMC5853577 | biostudies-literature

Identification of sugar transporter (SWEET) genes involved in pomegranate seed coat sugar accumulation.

Project description:Sugar content of the outer seed coat and hardness of the inner seed coat are important traits of the pomegranate fruit. The translocation of sugars across biological membranes, mediated by SWEET transporters, is critical to seed development. In this study, we identified 16 PgrSWEET genes distributed on six chromosomes in the pomegranate genome. According to the phylogenetic analysis, PgrSWEET proteins were divided into four groups. Tandem and segmental duplications contributed to the expansion of the PgrSWEET family, while functional redundancy and diversification may have occurred among SWEET members according to analyses of evolution and gene expression. RNA-seq and qRT-PCR analyses revealed that PgrSWEET1a and PgrSWEET9 were highly expressed in the inner seed coat, and the expression levels gradually increased during seed development. Moreover, the relative expression levels of PgrSWEET1a and PgrSWEET9 in a hard-seeded cultivar were higher than those in a soft-seeded cultivar, indicating that PgrSWEET1a and PgrSWEET9 might function in the inner seed coat development by accumulating sugar metabolites. We also found that PgrSWEET2 was highly expressed in the outer seed coat during seed development, and the protein was localized to the tonoplast, indicating that PgrSWEET2 is likely a candidate regulating sugar accumulation or reutilization in the vacuoles of the outer seed coat. Genes encoding transcription factors probably regulating the candidate PgrSWEET genes were chosen by co-expression analysis. These results not only helped to characterize PgrSWEET genes but also provided an insight into their functions in relation to seed coat development.Supplementary informationThe online version contains supplementary material available at 10.1007/s13205-022-03248-6.

| S-EPMC9296756 | biostudies-literature

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data