Search results for "synthesis"
showing 10 items of 2844 documents
Chapter 16 Folding and Pigment Binding of Light-Harvesting Chlorophyll a/b Protein (LHCIIb)
2010
The major light-harvesting chlorophyll a/b protein (LHCIIb) is one of the most abundant proteins of the chloroplast in green plants. It contains roughly half of the chlorophylls involved in photosynthesis, and exhibits an unusual ability to self-organize in vitro. Simply mixing the apoprotein, native or recombinant, with its pigments, chlorophyll a, chlorophyll b, and xanthophylls, in detergent solution, suffices to trigger protein folding and the assembly of about 18 pigments in their correct binding sites. A study of the mechanism of this self-organization seems worthwhile since (1) our knowledge about membrane protein folding is scarce compared to what we know about the folding of water-…
Hierarchical Imprinting Using Crude Solid Phase Peptide Synthesis Products as Templates
2003
The crude products resulting from solid-phase peptide synthesis can be used as epitope templates to generate surface-confined sites for the template and larger peptides containing the template motif. This offers a facile route to robust affinity stationary phases for the chromatographic separation of peptides.
Time- and concentration-dependent metabolic and genomic responses to exposure to resin acids in brown trout (Salmo trutta m. lacustris)
2006
The presence of metabolically conjugated resin acids (RAs) in the bile is considered to be a sensitive indicator for exposure of fish to pulp and paper industry effluents; however, to our knowledge, no comprehensive kinetic study of this response has been made. Juvenile brown trout (Salmo trutta m. lacustris) were exposed to a waterborne mixture of seven RAs (wood rosin) in time (0.1-192.0 h; average concentration, 8 microg/L) and dose (average concentrations, 0, 0.6, 4, 14, and 78 microg/L; 10 d) series, and total RAs were analyzed in bile. In time-dependent exposure, total RAs in bile increased up to 24 h. In concentration-dependent exposure, RAs increased along with the concentration of …
Cyclodextrin-assisted Glycan Chain Extension on a Protected Glycosyl Amino Acid
2000
By the use of cyclodextrins, we have enhanced the solubility of the protected amino acid glycan Fmoc-Thr(GalNAcα1)-OtBu (1b) up to 100-fold. This improvement enabled us to carry out an enzymatic glycosylation employing a β-galactosidase in combination with an α2,3-sialyltransferase without the aid of organic cosolvents. After optimization of the one-pot reaction, the sialylated core 1 structure Fmoc-Thr[Neu5Ac(α2-3)Gal(β1-3)GalNAcα1]-OtBu (3b) could be obtained with 50% yield.
Collagen overglycosylation: a biochemical feature that may contribute to bone quality.
2005
Skeletal ability to resist mechanical stress is determined by bone amount and quality, which relies on macro- and micro-architecture, turnover, bone matrix, and mineralisation; the role of collagen has not been clearly elucidated. Numerous post-translational steps are involved in collagen type I biosynthesis, including residue hydroxylation and glycosylation catalysed by enzymes that work until the protein folds forming the triple helix; therefore, folding rate regulates these processes. Overglycosylated hydroxylysines are poor substrates for epsilon-amino group deamination which initiates cross-link formation. Three clinical conditions associated with fractures may relate collagen overglyc…
C-Glycosyl amino acids through hydroboration-cross-coupling of exo-glycals and their application in automated solid-phase synthesis.
2013
O-Glycosylation is one of the most important post-translational modifications of proteins. The attachment of carbohydrates to the peptide backbone influences the conformation as well as the solubility of the conjugates and can even be essential for binding to specific ligands in cell-cell interactions or for active transport over membranes. This makes glycopeptides an interesting class of compounds for medical applications. To enhance the long-term availability of these molecules in vivo, the stabilization of the glycosidic bond between the amino acid residue and the carbohydrate is of interest. The described modular approach affords β-linked C-glycosyl amino acids by a sequence of Petasis …
Enzymatic glycosylation of o-glycopeptides
1992
Abstract O-Glycosylation of serine derivatives carried out with N-urethane protected glucosamine yields O-glycopeptides which are regio- and stereoselectively galactosylated with the aid of β-1,4-galactosyltransferase (EC 2.4.1.22).
Anodic Dehydrogenative Cyanamidation of Thioethers: Simple and Sustainable Synthesis of N‐Cyanosulfilimines
2021
Abstract A novel and very simple to perform electrochemical approach for the synthesis of several N‐cyanosulfilimines in good to excellent yields was established. This method provides access to biologically relevant sulfoximines by consecutive oxidation using electro‐generated periodate. This route can be easily scaled‐up to gram quantities. The S,N coupling is carried out at an inexpensive carbon anode by direct oxidation of sulfide. Therefore, the designed process is atom economic and represents a new “green route” for the synthesis of sulfilimines and sulfoximines.
Tailor‐Made Amino Acids and Fluorinated Motifs as Prominent Traits in Modern Pharmaceuticals
2020
Structural analysis of modern pharmaceutical practices allows for the identification of two rapidly growing trends: the introduction of tailor-made amino acids and the exploitation of fluorinated motifs. Curiously, the former represents one of the most ubiquitous classes of naturally occurring compounds, whereas the latter is the most xenobiotic and comprised virtually entirely of man-made derivatives. Herein, 39 selected compounds, featuring both of these traits in the same molecule, are profiled. The total synthesis, source of the corresponding amino acids and fluorinated residues, and medicinal chemistry aspects and biological properties of the molecules are discussed.
1H-nmr studies of polyoxyethylene-bound homo-oligo-L-methionines
1982
The use of 1H-nmr spectroscopy is demonstrated to be a useful analytical method to characterize the structure of synthetic peptides attached to soluble, macromolecular polyoxyethylene (POE) supports in the liquid-phase method (LPM) of peptide synthesis. We report an extensive 360-MHz 1H-nmr study of POE-bound homo-oligo-L-methionine peptides. A combination of high field and selective saturation or Redfield pulse methods allows resolution of individual backbone NH and α-CH resonances of dilute peptides in the presence of strong resonances from macromolecular POE and/or protonated solvents. The nmr spectra for the POE-bound peptides in CDCl3 are qualitatively similar to those of the low-molec…