Abstract: Provided herein are compounds having the structure of Formulas A-D and compositions thereof for use in the detection and quantification of viral neuraminidase. In particular, the compounds may be useful for the evaluation of viral strains and for vaccine evaluation.

Abstract: There are provided compounds of Formula I: various compositions thereof and methods for their use in the inhibition of ?-amylase.

Abstract: Provided herein are enzymatic compositions for protein O-glycosylation and sialylation, methods and systems associated therewith. In particular, the composition for in vivo sialylation of therapeutic proteins. The composition comprises a polypeptide N-acetylgalactosaminyltransferase; a ?-1,3-galactosyltransferase; an UDP-Glc/GlcNAc 4-epimerase; a disulfide bond isomerase; and an ?-2,3-sialyltransferase or an ?-2,6-sialyltransferase. Furthermore, provided herein are compositions for efficient and complete O-glycosylation and di-sialylation of therapeutic proteins.

Abstract: Provided herein are perfusion fluids for enzymatically cleaving A-antigens from a donor organ, and methods, uses, associated therewith. In particular, the perfusion fluids comprise two enzymes, GalNAcDeacetylase and Galactosaminidase and the fluids may further comprise a buffered extracellular solution and/or a crowing agent. Furthermore, the compositions described herein were found to have activity at temperatures and pH levels suitable for cell viability.

Abstract: Provided herein are enzymatic compositions for carbohydrate antigen cleavage, methods, uses, apparatuses and systems associated therewith. In particular, the composition comprises two enzymes, GalNAcDeacetylase and Galactosaminidase and the composition may further comprise a crowding agent. Furthermore, the compositions described herein were found to have activity a temperatures and pH levels suitable for cell viability.

Abstract: There are provided compounds of Formula I: various compositions thereof and methods for their use in the inhibition of ?-amylase.

Abstract: Provided are methods, uses and pharmaceutical compositions for inhibition of mammalian alpha-amylase in a subject, with a Helianthamide peptide or a derivative thereof in a biologically effective amount. The subject in need of alpha-amylase inhibition, may have or be at risk of developing one or more of the following: Middleton syndrome; a motility disorder of the gastrointestinal tract; postprandial reactive hypoglycemia; postprandial syndrome; irritable bowel syndrome; diabetes mellitus type 1; diabetes mellitus type 2; pre-diabetes; obesity, dumping syndrome; infant dumping syndrome; polycystic ovary syndrome; steatohepatitis; and viral infection.

Abstract: Provided herein are compounds having the structure of Formulas A-D and compositions thereof for use in the detection and quantification of viral neuraminidase. In particular, the compounds may be useful for the evaluation of viral strains and for vaccine evaluation.

Abstract: This invention discloses the use of aminoglycoside antibiotics such as gentamicin B1 to suppress premature termination codons during translation and promote the full length read-through of transcripts such as p53 that incorporate nonsense mutations and to treat disease conditions such as cancer caused by such genetic mutations.

Abstract: This invention provides compound having a structure of Formulas: Furthermore, methods and uses of such compounds for covalently bonding to a sugar acceptor, to form modified protein therapeutics having reduced enzymatic hydrolysis, improved biological stability or an improved pharmacokinetic property.

Abstract: Provided are methods, uses and pharmaceutical compositions for inhibition of mammalian alpha-amylase in a subject, with a Helianthamide peptide or a derivative thereof in a biologically effective amount. The subject in need of alpha-amylase inhibition, may have or be at risk of developing one or more of the following: Middleton syndrome; a motility disorder of the gastrointestinal tract; postprandial reactive hypoglycemia; postprandial syndrome; irritable bowel syndrome; diabetes mellitus type 1; diabetes mellitus type 2; pre-diabetes; obesity, dumping syndrome; infant dumping syndrome; polycystic ovary syndrome; steatohepatitis; and viral infection.

Abstract: This invention provides compound having a structure of Formulas: Furthermore, methods and uses of such compounds for covalently bonding to a sugar acceptor, to form modified protein therapeutics having reduced enzymatic hydrolysis, improved biological stability or an improved pharmacokinetic property.

Abstract: Mutant glycosidase enzymes are formed in which the normal nucleophilic amino acid within the active site has been changed to a nonnucleophilic amino acid. These enzymes cannot hydrolyze disaccharide products, but which can still form them. Using this enzyme, oligosaccharides are synthesized by preparing a mixture of an &agr;glycosyl fluoride and a glycoside acceptor molecule; enzymatically coupling the &agr.glycosyl fluoride to the glycoside acceptor molecule to form a glycosyl glycoside product using the mutant glycosidase enzyme; and recovering the glycosyl glycoside product. Particular enzymes include a mutant form of Agrobacterium &bgr.Glucosidase in which the normal glutamic acid residue at position 358 is replaced with an alanine residue.

Abstract: The present invention relates to a crystal comprising the ligand binding pocket of a glycosyltransferase enzyme and optionally a donor molecule or analogue thereof and/or an acceptor molecule or analogue thereof. The present invention also relates to the use of such a crystal to identify ligands capable of modulating glycosyltransferase activity, and the use of such ligands in therapeutic applications.

Abstract: The present invention provides materials and methods for the solid-phase synthesis of oligosaccharides and glycopeptides. Such materials and methods include mutant glycosidase enzymes, or “glycosynthases,” chemically-derivatized acceptor molecules, and specific solid support matrices.

Abstract: Mutant glycosidase enzymes are formed in which the normal nucleophilic amino acid within the active site has been changed to a nonnucleophilic amino acid. These enzymes cannot hydrolyze disaccharide products, but which can still form them. Using this enzyme, oligosaccharides are synthesized by preparing a mixture of an &agr;glycosyl fluoride and a glycoside acceptor molecule; enzymatically coupling the &agr.glycosyl fluoride to the glycoside acceptor molecule to form a glycosyl glycoside product using the mutant glycosidase enzyme; and recovering the glycosyl glycoside product. Particular enzymes include a mutant form of Agrobacterium &bgr.Glucosidase in which the normal glutamic acid residue at position 358 is replaced with an alanine residue.

Abstract: Mutant glycosidase enzymes are formed in which the normal nucleophilic amino acid within the active site has been changed to a non-nucleophilic amino acid. These enzymes cannot hydrolyze disaccharide products, but which can still form them. Using this enzyme, oligosaccharides are synthesized by preparing a mixture of an &agr;-glycosyl fluoride and a glycoside acceptor molecule; enzymatically coupling the &agr;-glycosyl fluoride to the glycoside acceptor molecule to form a glycosyl glycoside product using the mutant glycosidase enzyme; and recovering the glycosyl glycoside product. Particular enzymes include a mutant form of Agrobacterium &bgr;-Glucosidase in which the normal glutamic acid residue at position 358 is replaced with an alanine residue.

Abstract: Glycosylated acceptors are prepared using glycosyl transferase and activated glycosyl derivatives as donor sugars without the use of sugar nucleotides as donor sugars. A reaction mixture composition containing an activated glycoside derivative such as glycosyl fluoride or glycosyl mesylate, an acceptor substrate such as lactose or other oligosaccharide, a glycosyl transferase and a catalytic amount of a nucleotide phosphate or nucleotide phosphate analog is reacted to produce the glycosylated acceptor. The acceptor substrate may also be a monosaccharide, a fluorescent-labeled saccharide or a saccharide derivative such as an aminoglycoside antibiotic. The glycosyl transferase may be immobilized by removing its membrane-binding domain and attaching in its place a cellulose-binding domain. In another embodiment, a glycosylated acceptor is formed by making a nucleotide phosphate glycoside in situ in a steady state concentration.

Abstract: Oligosaccharides are prepared using glycosyl transferase and activated glycosyl derivatives as donor sugars without the use of sugar nucleotides as donor sugars. A reaction mixture composition containing an activated glycoside derivative such as glycosyl fluoride or glycosyl mesylate, an acceptor substrate such as lactose or other oligosaccharide, a glycosyl transferase and a catalytic amount of a nucleotide phosphate or nucleotide phosphate analog is reacted to produce a glycosylated acceptor. In addition to an oligosaccharide, the acceptor substrate may be a monosaccharide, a fluorescent-labeled saccharide or a saccharide derivative such as an aminoglycoside antibiotic. The glycosyl transferase may be immobilized by removing its membrane-binding domain and attaching in its place a cellulose-binding domain. In a preferred embodiment, galactosyl transferase is the glycosyl transferase, .alpha.-D-galactosyl fluoride is the activated glycoside derivative and lactose is the acceptor substrate.

Abstract: Mutant glycosidase enzymes are formed in which the normal nucleophilic amino acid within the active site has been changed to a non-nucleophilic amino acid. These enzymes cannot hydrolyze disaccharide products, but can still form them. Using this enzyme, oligosaccharides are synthesized by preparing a mixture of an .alpha.-glycosyl fluoride and a glycoside acceptor molecule; enzymatically coupling the .alpha.-glycosyl fluoride to the glycoside acceptor molecule to form a glycosyl glycoside product using the mutant glycosidase enzyme; and recovering the glycosyl glycoside product. Particular enzymes include a mutant form of Agrobacterium .beta.-Glucosidase in which the normal glutamic acid residue at position 358 is replaced with an alanine residue.