A5035483275- Silk-based biomaterials and applications
- Biochemical and Structural Characterization
- Alzheimer's disease research and treatments
- Biotin and Related Studies
- Prion Diseases and Protein Misfolding
- Protein Structure and Dynamics
- Supramolecular Self-Assembly in Materials
- biodegradable polymer synthesis and properties
- Bacterial biofilms and quorum sensing
- Proteins in Food Systems
- Mass Spectrometry Techniques and Applications
- Bacillus and Francisella bacterial research
- Enzyme Structure and Function
- Insect Resistance and Genetics
- Trace Elements in Health
- Cellular Mechanics and Interactions
- Chemical Synthesis and Analysis
- Diatoms and Algae Research
- Protein purification and stability
- Silkworms and Sericulture Research
- Antimicrobial Peptides and Activities
- Invertebrate Immune Response Mechanisms
- Advanced Fluorescence Microscopy Techniques
- Advanced Proteomics Techniques and Applications
- Cell Adhesion Molecules Research
Laboratoire des Matériaux et du Génie Physique
2013-2024
Institut polytechnique de Grenoble
2013-2024
Laboratoire de Recherche sur la Croissance Cellulaire, la Réparation et la Régénération Tissulaires
2015-2024
CY Cergy Paris Université
2010-2024
Equipes Traitement de l'Information et Systèmes
2018
BP (France)
2018
Centre National de la Recherche Scientifique
2015-2016
Université Grenoble Alpes
2005-2013
European Synchrotron Radiation Facility
2008-2011
Laboratoire de Chimie et Biologie des Métaux
2011
We have characterized the steps involved in silk assembly from protein solution into β-type fibers by a combination of small-angle and wide-angle X-ray scattering Raman spectroscopy. The aggregation process was studied concentric flow microfluidic cell, which allows mimicking spinning duct. fibroin molecule shows an elongated shape with maximum diameter 38 nm. During pH-driven initial step, large-scale aggregates molecules about 260 nm are formed. spectroscopy on dried, fibrous material...
Abstract Amyloid fibrils are self‐assembled protein structures with important roles in biology (either pathogenic or physiological), and attracting increasing interest nanotechnology. However, because of their high aspect ratio the presence some polymorphism, that is, possibility to adopt various structures, characterization is challenging basic information such as mass unknown. Here we show charge‐detection spectrometry, recently developed for large systems viruses, provides a...
Several studies have suggested the implication of classical complement pathway in early stages prion disease pathogenesis. To explore this hypothesis, surface plasmon resonance spectroscopy was used to test ability human C1q recognize mouse PrP immobilized on a sensor chip. In configuration, bound avidly PrP, with KD 5.4 nM (kon = 2.4 × 105 M-1 s-1; koff 1.3 10-3 s-1). The isolated globular domain also although higher (238 nM), due decreased kon (4.2 103 Interaction strongly enhanced by Cu2+...
Abstract Regenerated silkworm fibers spun through a wet‐spinning process followed by an immersion postspinning drawing step show work to fracture comparable with that of natural silk in wide range spinning conditions. The mechanical behavior and microstructure these high performance have been characterized, compared those produced conventional comparison reveals both sets share common semicrystalline microstructure, but significant differences are apparent the amorphous region. Besides,...
Characterization by charge detection mass spectrometry of amyloid fibers involved in neurodegenerative diseases: Aβ peptide, tau and α-synuclein.
Biofilm associated proteins (Bap) are involved in the biofilm formation process of several bacterial species. The sequence STVTVT is present Bap expressed by many Staphylococcus species, Acinetobacter baumanii and Salmonella enterica. peptide STVTVTF derived from C-repeat protein epidermidis was selected through AGGRESCAN, PASTA, TANGO software prediction aggregation amyloid fibers. We characterized self-assembly properties different methods: presence peptide, we observed an increase...
The bacterial biofilm is a complex environment of cells, which secrete matrix made various components, mainly polysaccharides and proteins. An understanding the precise role these components in stability dynamics architecture would be great advantage for improvement anti-biofilm strategies. Here, artificial matrices auto-assembled peptides were designed, influence amyloid proteins on mechanical properties was studied. model methylcellulose alginate derived from curli FapC found biofilms...
We have studied a cast fibroin drop with grazing incidence small-angle X-ray scattering, imaging, and spectroscopy techniques. Optical microscopy shows that the dried forms boundary zone. Grazing-incidence scattering performed synchrotron radiation microbeam in zone suggests formation of nanometer-sized domains one-dimensional paracrystalline order. Atomic force scanning electron support nanofibrillar morphology. MicroRaman beta-sheet secondary structure zone, which is attributed to shearing...
The operon containing the genes encoding subunits of binary crystal toxin Bacillus sphaericus strain LP1-G, BinA and BinB (41.9 kDa 51.4 kDa, respectively), was cloned sequenced. Purified crystals were not toxic to Culex pipiens larvae. Comparison amino-acid sequences this (Bin4) with those three other known types (Bin1, Bin2 Bin3) revealed mutations at six positions, including a serine position 93 BinA4, whereas all from B. had leucine position. Reciprocal site-directed mutagenesis...
The objective of this study was to determine the effect size-fractionation by centrifugation on film structure casein micelles. Fractionated micelles in solution were asymmetrically distributed with a small distribution width as measured dynamic light scattering. Films prepared from size-fractionated samples showed smooth surface optical microscopy images and homogeneous microstructure atomic force micrographs. nano- films probed micro-beam grazing incidence angle x-ray scattering (μGISAXS)....
Interactions between proteins and material or cellular surfaces are able to trigger protein aggregation in vitro vivo. The human insulin peptide segment LVEALYL is accelerate the presence of hydrophobic surfaces. We show that this needs be previously adsorbed on a surface induce aggregation. Moreover, study different mutant peptides proves its sequence less important than secondary structure surface. Indeed, these pro‐aggregative act by providing stable β‐sheets incoming molecules, thereby...
Amyloid fibrils are self-assembled protein structures with important roles in biology (either pathogenic or physiological), and attracting increasing interest nanotechnology. However, because of their high aspect ratio the presence some polymorphism, that is, possibility to adopt various structures, characterization is challenging basic information such as mass unknown. Here we show charge-detection spectrometry, recently developed for large systems viruses, provides a straightforward manner.
ADVERTISEMENT RETURN TO ISSUEPREVNoteNEXTSilk Fiber Formation after High-Pressure Treatment of Fibroin Solution in a Diamond Anvil CellRonald Gebhardt, Charlotte Vendrely†, Michael Hanfland, and Christian Riekel*View Author Information European Synchrotron Radiation Facility, B.P. 220, F-38043 Grenoble Cedex, France* To whom correspondence should be addressed.†Present address: Université de Cergy-Pontoise, ERRMECE, F-95000, France.Cite this: Macromolecules 2008, 41, 24, 9934–9936Publication...
We characterized the formation of amyloid fibers by two peptides derived from CsgA sequence: R5 (133- 151) corresponding to whole repeating unit and a truncated form this peptide called R5T (134-143). In presence either peptides: an increase in fluorescence intensity Thioflavin T was observed; shift absorbance Congo red measured; spontaneous observed polarized light as well asatomic force microscopy imaging. Large-size aggregates were with while formed fagots individualized fibers. The...