4 results on '"Gasset, Maria"'
Search Results
2. Boronate complex formation with Dopa containing mussel adhesive protein retards ph-induced oxidation and enables adhesion to mica
- Author
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J. Herbert Waite, Yunfei Chen, Jacob N. Israelachvili, Eric Danner, Yajing Kan, and Gasset, Maria
- Subjects
General Science & Technology ,Materials Science ,Biophysics ,lcsh:Medicine ,02 engineering and technology ,010402 general chemistry ,Biochemistry ,Protein Chemistry ,01 natural sciences ,Redox ,Biomaterials ,Acetic acid ,chemistry.chemical_compound ,Adhesives ,Oxidation ,Oxidizing agent ,Polymer chemistry ,Animals ,Post-Translational Modification ,Protein Interactions ,lcsh:Science ,chemistry.chemical_classification ,Multidisciplinary ,Chemistry ,Physics ,lcsh:R ,Chemical Reactions ,Proteins ,Biology and Life Sciences ,Polymer ,Adhesion ,021001 nanoscience & nanotechnology ,Boronic Acids ,Dihydroxyphenylalanine ,0104 chemical sciences ,Amino acid ,Mollusca ,Covalent bond ,Physical Sciences ,Aluminum Silicates ,lcsh:Q ,Structural Proteins ,Adhesive ,0210 nano-technology ,Research Article ,Biotechnology - Abstract
© 2014 Kan et al. The biochemistry of mussel adhesion has inspired the design of surface primers, adhesives, coatings and gels for technological applications. These mussel-inspired systems often focus on incorporating the amino acid 3,4-dihydroxyphenyl-L-alanine (Dopa) or a catecholic analog into a polymer. Unfortunately, effective use of Dopa is compromised by its susceptibility to auto-oxidation at neutral pH. Oxidation can lead to loss of adhesive function and undesired covalent cross-linking. Mussel foot protein 5 (Mfp-5), which contains ∼30 mole % Dopa, is a superb adhesive under reducing conditions but becomes nonadhesive after pH-induced oxidation. Here we report that the bidentate complexation of borate by Dopa to form a catecholato-boronate can be exploited to retard oxidation. Although exposure of Mfp-5 to neutral pH typically oxidizes Dopa, resulting in a
- Published
- 2014
3. A novel metagenomic short-chain dehydrogenase/reductase attenuates Pseudomonas aeruginosa biofilm formation and virulence on Caenorhabditis elegans
- Author
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Hinrich Schulenburg, Wolfgang R. Streit, Hubert Mayerhofer, Patrick Bijtenhoorn, Jochen Müller-Dieckmann, Stephanie Grond, Rolf Daniel, Katja Dierking, Christina Schipper, Andrea Thürmer, Elzbieta Brzuszkiewicz, Matthias Szesny, Christian Utpatel, Claudia Hornung, and Gasset, Maria
- Subjects
Bacterial Diseases ,Reductase ,medicine.disease_cause ,Biochemistry ,chemistry.chemical_compound ,Molecular Cell Biology ,0303 health sciences ,Multidisciplinary ,Virulence ,Enzyme Classes ,Quorum Sensing ,food and beverages ,Animal Models ,Enzymes ,Infectious Diseases ,Quorum Quenching ,biofilm ,bacteria ,Caenorhabditis elegans ,Pseudomonas aeruginosa ,Medicine ,Oxidoreductases ,Research Article ,Signal Transduction ,Science ,Biology ,Microbiology ,Molecular Genetics ,03 medical and health sciences ,Pyocyanin ,Model Organisms ,Bacterial Proteins ,medicine ,Genetics ,Animals ,Gene Regulation ,Pseudomonas Infections ,030304 developmental biology ,030306 microbiology ,Gene Expression Profiling ,Biofilm ,Bacteriology ,biochemical phenomena, metabolism, and nutrition ,Quorum sensing ,chemistry ,Biofilms ,Pyocyanine ,Heterologous expression ,Metagenomics ,Bacterial Biofilms ,NADP - Abstract
In Pseudomonas aeruginosa, the expression of a number of virulence factors, as well as biofilm formation, are controlled by quorum sensing (QS). N-Acylhomoserine lactones (AHLs) are an important class of signaling molecules involved in bacterial QS and in many pathogenic bacteria infection and host colonization are AHL-dependent. The AHL signaling molecules are subject to inactivation mainly by hydrolases (Enzyme Commission class number EC 3) (i.e. N-acyl-homoserine lactonases and N-acyl-homoserine-lactone acylases). Only little is known on quorum quenching mechanisms of oxidoreductases (EC 1). Here we report on the identification and structural characterization of the first NADP-dependent short-chain dehydrogenase/reductase (SDR) involved in inactivation of N-(3-oxo-dodecanoyl)-L-homoserine lactone (3-oxo-C(12)-HSL) and derived from a metagenome library. The corresponding gene was isolated from a soil metagenome and designated bpiB09. Heterologous expression and crystallographic studies established BpiB09 as an NADP-dependent reductase. Although AHLs are probably not the native substrate of this metagenome-derived enzyme, its expression in P. aeruginosa PAO1 resulted in significantly reduced pyocyanin production, decreased motility, poor biofilm formation and absent paralysis of Caenorhabditis elegans. Furthermore, a genome-wide transcriptome study suggested that the level of lasI and rhlI transcription together with 36 well known QS regulated genes was significantly (≥10-fold) affected in P. aeruginosa strains expressing the bpiB09 gene in pBBR1MCS-5. Thus AHL oxidoreductases could be considered as potent tools for the development of quorum quenching strategies.
- Published
- 2011
4. Systematic Exploitation of Multiple Receptor Conformations for Virtual Ligand Screening
- Author
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Giovanni Bottegoni, Ruben Abagyan, Walter Rocchia, Andrea Cavalli, Manuel Rueda, Bottegoni G., Rocchia W., Rueda M., Abgyan R., Cavalli A, and Gasset, Maria
- Subjects
Protein Conformation ,lcsh:Medicine ,Ligands ,Bioinformatics ,Biochemistry ,Computational Chemistry ,Protein structure ,Receptors ,Drug Discovery ,Macromolecular Structure Analysis ,Combinatorial Chemistry Techniques ,Biomacromolecule-Ligand Interactions ,lcsh:Science ,Protocol (object-oriented programming) ,Multidisciplinary ,Drug discovery ,Chemistry ,Physics ,Cell Surface ,Medicine ,Biophysic Al Simulations ,Algorithms ,Research Article ,Biotechnology ,Protein Binding ,Protein Structure ,Drugs and Devices ,Drug Research and Development ,General Science & Technology ,Biophysics ,Receptors, Cell Surface ,Computational biology ,Protein Chemistry ,Chemical Biology ,Humans ,Set (psychology) ,Biology ,Flexibility (engineering) ,Virtual screening ,Ligand ,lcsh:R ,Proteins ,Computational Biology ,Small Molecules ,Drug Design ,lcsh:Q ,Generic health relevance ,Medicinal Chemistry - Abstract
The role of virtual ligand screening in modern drug discovery is to mine large chemical collections and to prioritize for experimental testing a comparatively small and diverse set of compounds with expected activity against a target. Several studies have pointed out that the performance of virtual ligand screening can be improved by taking into account receptor flexibility. Here, we systematically assess how multiple crystallographic receptor conformations, a powerful way of discretely representing protein plasticity, can be exploited in screening protocols to separate binders from non-binders. Our analyses encompass 36 targets of pharmaceutical relevance and are based on actual molecules with reported activity against those targets. The results suggest that an ensemble receptor-based protocol displays a stronger discriminating power between active and inactive molecules as compared to its standard single rigid receptor counterpart. Moreover, such a protocol can be engineered not only to enrich a higher number of active compounds, but also to enhance their chemical diversity. Finally, some clear indications can be gathered on how to select a subset of receptor conformations that is most likely to provide the best performance in a real life scenario.
- Published
- 2011
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