Search

Your search keyword '"Caliandro, Rosanna"' showing total 14 results
Start Over Author "Caliandro, Rosanna" Publication Year Range Last 10 years
14 results on '"Caliandro, Rosanna"'

3. Novel tacrine-tryptophan hybrids: Multi-target directed ligands as potential treatment for Alzheimer's disease

Author

Chalupova, Katarina, Korabecny, Jan, Bartolini, Manuela, Monti, Barbara, Lamba, Doriano, Caliandro, Rosanna, Pesaresi, Alessandro, Brazzolotto, Xavier, Gastellier, Anne-Julie, Nachon, Florian, Pejchal, Jaroslav, Jarosova, Michaela, Hepnarova, Vendula, Jun, Daniel, Hrabinova, Martina, Dolezal, Rafael, Zdarova Karasova, Jana, Mzik, Martin, Kristofikova, Zdena, Misik, Jan, Muckova, Lubica, Jost, Petr, Soukup, Ondrej, Benkova, Marketa, Setnicka, Vladimir, Habartova, Lucie, Chvojkova, Marketa, Kleteckova, Lenka, Vales, Karel, Mezeiova, Eva, Uliassi, Elisa, Valis, Martin, Nepovimova, Eugenie, Bolognesi, Maria Laura, and Kuca, Kamil

Published
2019
Full Text
View/download PDF

5. Crystal structure report of the ImmR transcriptional regulator DNA-binding domain of the Bacillus subtilis ICEBs1 transposon

Author

Generalitat de Catalunya, Ministerio de Ciencia, Innovación y Universidades (España), Agencia Estatal de Investigación (España), Fundació La Marató de TV3, Caliandro, Rosanna, Diego, Iñaki de, Gomis-Rüth, F. Xavier, Generalitat de Catalunya, Ministerio de Ciencia, Innovación y Universidades (España), Agencia Estatal de Investigación (España), Fundació La Marató de TV3, Caliandro, Rosanna, Diego, Iñaki de, and Gomis-Rüth, F. Xavier

Abstract

Bacillus subtilis is a commensal member of the human oral and gut microbiomes, which can become infectious to immunocompromised patients. It possesses a conjugative transposon, ICEBs1, which includes > 20 genes and can be passed by horizontal gene transfer to other bacteria, including pathogenic Bacillus anthracis and Listeria monocytogenes. ICEBs1 is regulated by the ImmR/ImmA tandem, which are a transcriptional repressor that constitutively blocks transcription and a metallopeptidase that acts as anti-repressor and inactivates ImmR by proteolytic cleavage. We here report the production and purification of 127-residue ImmR from ICEBs1 and the crystal structure of its DNA-binding domain. It features a five-helix bundle centred on a helix-turn-helix motif potentially binding the major grove of double-stranded target DNA. ImmR shows structural and mechanistic similarity with the B. subtilis SinR repressor, which is engaged in sporulation inhibition.

Published
2022

12. The Structure of Sucrose-Soaked Levansucrase Crystals from Erwinia tasmaniensis reveals a Binding Pocket for Levanbiose.

Author

Polsinelli, Ivan, Caliandro, Rosanna, Demitri, Nicola, and Benini, Stefano

Subjects
*ERWINIA, *FRUCTOOLIGOSACCHARIDES, *CRYSTAL structure, *GRAM-negative bacteria, *BIOENGINEERING, *PREBIOTICS, *CRYSTALS
Abstract

Given its potential role in the synthesis of novel prebiotics and applications in the pharmaceutical industry, a strong interest has developed in the enzyme levansucrase (LSC, EC 2.4.1.10). LSC catalyzes both the hydrolysis of sucrose (or sucroselike substrates) and the transfructosylation of a wide range of acceptors. LSC from the Gram-negative bacterium Erwinia tasmaniensis (EtLSC) is an interesting biocatalyst due to its high-yield production of fructooligosaccharides (FOSs). In order to learn more about the process of chain elongation, we obtained the crystal structure of EtLSC in complex with levanbiose (LBS). LBS is an FOS intermediate formed during the synthesis of longer-chain FOSs and levan. Analysis of the LBS binding pocket revealed that its structure was conserved in several related species. The binding pocket discovered in this crystal structure is an ideal target for future mutagenesis studies in order to understand its biological relevance and to engineer LSCs into tailored products. [ABSTRACT FROM AUTHOR]

Published
2020
Full Text
View/download PDF

13. DISCOVERY AND CHARACTERIZATION OF TACRINE/HUPRINE-TRYPTOPHAN HETERODIMERS AS NOVEL MULTIPOTENT COMPOUNDS AGAINST ALZHEIMER'S DISEASE.

Author

Korabecny, Jan, Spilovska, Katarina, Bartolini, Manuela, Monti, Barbara, Lamba, Doriano, Caliandro, Rosanna, Pesaresi, Alessandro, Hepnarova, Vendula, Jun, Daniel, Hrabinova, Martina, Dolezal, Rafael, Karasova, Jana Zdarova, Soukup, Ondrej, Mezeiova, Eva, Nepovimova, Eugenie, Bolognesi, Maria Laura, and Kuca, Kamil

Subjects
TACRINE, HETERODIMERS, MULTIPOTENT stem cells, ALZHEIMER'S disease, TRYPTOPHAN, DRUG design
Abstract

Combination of tacrine/huprine, connected through a different linker tether length, with tryptophan led to the generation of a novel, highly-potent family of multi-target directed ligands targeting key molecular mechanisms of Alzheimer's disease. Based on in vitro biological profile, the 6-chloro-tacrine-(CH2)6-L-tryptophan heterodimer S- K1035 was found to be the most potent inhibitor of human acetylcholinesterase (hAChE) and human butyrylcholinesterase (hBChE) within the series, with nanomolar IC50 values (6.31 and 9.07 nM, respectively). Moreover, S K1035 showed good ability to inhibit Aß42 self-aggregation and hAChE-induced Aß40 aggregation. The X-ray crystallographic analysis of TcAChE in complex with S-K1035 highlighted the utility of the hybridization approach used in the structure based drug design. S K1035 also exerted moderate inhibition against neuronal nitric oxide synthase (nNOS). In vivo studies displayed low toxicity profile compared to parent tacrine. S-K1035 also significantly ameliorated performances of scopolamine-treated animals. [ABSTRACT FROM AUTHOR]

Published
2018

14. The structural and functional characterization of Malus domestica double bond reductase MdDBR provides insights towards the identification of its substrates

Author

Stefano Benini, Nicola Demitri, Ivan Polsinelli, Francesco Musiani, Stefan Martens, Rosanna Caliandro, Caliandro, Rosanna, Polsinelli, Ivan, Demitri, Nicola, Musiani, Francesco, Martens, Stefan, and Benini, Stefano

Subjects
Models, Molecular, Protein Conformation, alpha-Helical, Arabidopsis, Gene Expression, Dehydrogenase, 02 engineering and technology, Reductase, Crystallography, X-Ray, Biochemistry, Substrate Specificity, chemistry.chemical_compound, αβ-unsaturated double bond, NADPH-dependent reduction, Structural Biology, Cloning, Molecular, Plant Proteins, chemistry.chemical_classification, 0303 health sciences, Phenylpropanoid, Dihydrochalcone, General Medicine, 021001 nanoscience & nanotechnology, Butanones, Recombinant Proteins, Malus, β-unsaturated double bond, Thermodynamics, Oxidoreductases, 0210 nano-technology, Protein Binding, Double bond, Stereochemistry, Genetic Vectors, α, Double bond reductase, 03 medical and health sciences, Biosynthesis, Tobacco, Escherichia coli, Protein Interaction Domains and Motifs, Amino Acid Sequence, Settore BIO/10 - BIOCHIMICA, Molecular Biology, Phenylpropanoid pathway, 030304 developmental biology, Binding Sites, Sequence Homology, Amino Acid, Apple, Substrate (chemistry), X-ray crystal structure, Kinetics, Enzyme, chemistry, Protein Conformation, beta-Strand, Apoproteins, Rubus, Sequence Alignment, NADP
Abstract

In this study we describe the crystal structures of the apoform, the binary and the ternary complexes of a double bond reductase from Malus domestica L. (MdDBR) and explore a range of potential substrates. The overall fold of MdDBR is similar to that of the medium chain reductase/dehydrogenase/zinc-dependent alcohol dehydrogenase-like family. Structural comparison of MdDBR with Arabidopsis thaliana DBR (AtDBR), Nicotiana tabacum DBR (NtDBR) and Rubus idaeus DBR (RiDBR) allowed the identification of key amino acids involved in cofactor and ligands binding and shed light on how these residues may guide the orientation of the substrates. The enzyme kinetic for the substrate trans-4-phenylbuten-2-one has been analyzed, and MdDBR activity towards a variety of substrates was tested. This enzyme has been reported to be involved in the phenylpropanoid pathway where it would catalyze the NADPH-dependent reduction of the α, β-unsaturated double bond of carbonyl metabolites. Our study provides new data towards the identification of MdDBR natural substrate and the biosynthetic pathway where it belongs. Furthermore, the originally proposed involvement in dihydrochalcone biosynthesis in apple must be questioned.

Published
2021
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results