Preparation of 3-methoxycarbonylpropyl α-<scp>D</scp>- and 7-methoxycarbonylhexyl β-<scp>D</scp>-galactopyranosides: spacer-arm glycosides for branched oligosaccharide synthesis

Collins, Peter; Eder, Hansjörg

doi:10.1039/p19840001525

Cited by 10 publications

(2 citation statements)

References 7 publications

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“…(A) 2-Benzyloxyethanol (3a): bp 90-95 °C/0.7 mmHg (62%). (E) 6-Benzyloxy-1-hexanol (3e) (38)(39)(40)(41)(42)(43): bp 115-120 °C/ 0.7 mmHg (63%). 1 H NMR δ 7.26-7.35 (m, 5H), 4.50 (s, 2H), 3.62 (t, 2H, J ) 6.6 Hz), 3.47 (t, 2H, J ) 6.2 Hz), 1.36-1.65 (m, 9H); 13 C NMR δ 138.…”

Section: Methodsmentioning

confidence: 99%

Protein Farnesyltransferase Isoprenoid Substrate Discrimination Is Dependent on Isoprene Double Bonds and Branched Methyl Groups

Micali

et al. 2001

Biochemistry

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Farnesylation is a posttranslational lipid modification in which a 15-carbon farnesyl isoprenoid is linked via a thioether bond to specific cysteine residues of proteins in a reaction catalyzed by protein farnesyltransferase (FTase). We synthesized the benzyloxyisoprenyl pyrophosphate (BnPP) series of transferable farnesyl pyrophosphate (FPP) analogues (1a-e) to test the length dependence of the isoprenoid substrate on the FTase-catalyzed transfer of lipid to protein substrate. Kinetic analyses show that pyrophosphates 1a-e and geranyl pyrophosphate (GPP) transfer with a lower efficiency than FPP whereas geranylgeranyl pyrophosphate (GGPP) does not transfer at all. While a correlation was found between K(m) and analogue hydrophobicity and length, there was no correlation between k(cat) and these properties. Potential binding geometries of FPP, GPP, GGPP, and analogues 1a-e were examined by modeling the molecules into the active site of the FTase crystal structure. We found that analogue 1d displaces approximately the same volume of the active site as does FPP, whereas GPP and analogues 1a-c occupy lesser volumes and 1e occupies a slightly larger volume. Modeling also indicated that GGPP adopts a different conformation than the farnesyl chain of FPP, partially occluding the space occupied by the Ca(1)a(2)X peptide in the ternary X-ray crystal structure. Within the confines of the FTase pocket, the double bonds and branched methyl groups of the geranylgeranyl chain significantly restrict the number of possible conformations relative to the more flexible lipid chain of analogues 1a-e. The modeling results also provide a molecular explanation for the observation that an aromatic ring is a good isostere for the terminal isoprene of FPP.

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Section: Methodsmentioning

confidence: 99%

Protein Farnesyltransferase Isoprenoid Substrate Discrimination Is Dependent on Isoprene Double Bonds and Branched Methyl Groups

Micali

et al. 2001

Biochemistry

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“…Then, reductive amination is performed using an aldehydic sugar derived from galactose: the galactopyranosylethanal. This sugar is easily prepared in two steps according to conditions previously described in literature with some modifications (Scheme 7) [31,32].…”

Section: Glycosylated Nanoparticules Using Reductive Aminationmentioning

confidence: 99%

Synthesis and characterization of glycosylated nano particles

et al. 2006

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Functionalized polymer nanoparticles have been synthesized by emulsifier-free emulsion polymerization of styrene with amino-functionalized monomers.Two monomers were used: the well-known 2-aminoethylmethacrylate and a new monomer with a styrenic polymerizable function, 4-(2-aminoethylthio)methylstyrene. The latexes were characterized by gravimetry, dynamic light scattering and colorimetric titration in order to obtain the styrene conversion, the hydrodynamic diameter, the particle size distribution and the concentration of surface amino groups, respectively. Then, glycosydic molecules such as maltose, lactose, maltotriose and galactopyranosylethanal were covalently grafted to the nanoparticles by amidation or reductive amination.

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ChemInform Abstract: PREPARATION OF 3‐METHOXYCARBONYLPROPYL α‐D‐ AND 7‐METHOXYCARBONYLHEPTYL β‐D‐GALACTOPYRANOSIDES: SPACER‐ARM GLYCOSIDES FOR BRANCHED OLIGOSACCHARIDE SYNTHESIS

Collins¹,

Eder²

1984

Chemischer Informationsdienst

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Preparation of 3-methoxycarbonylpropyl α-D- and 7-methoxycarbonylhexyl β-D-galactopyranosides: spacer-arm glycosides for branched oligosaccharide synthesis

Cited by 10 publications

References 7 publications

Protein Farnesyltransferase Isoprenoid Substrate Discrimination Is Dependent on Isoprene Double Bonds and Branched Methyl Groups

Protein Farnesyltransferase Isoprenoid Substrate Discrimination Is Dependent on Isoprene Double Bonds and Branched Methyl Groups

Synthesis and characterization of glycosylated nano particles

ChemInform Abstract: PREPARATION OF 3‐METHOXYCARBONYLPROPYL α‐D‐ AND 7‐METHOXYCARBONYLHEPTYL β‐D‐GALACTOPYRANOSIDES: SPACER‐ARM GLYCOSIDES FOR BRANCHED OLIGOSACCHARIDE SYNTHESIS

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