Neuraminidase Inhibitors
SEE ALSO...
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
N-Acetyl-2,3-dehydro-2-deoxyneuraminic Acid, Sodium Salt | 209977-53-7 | sc-221978A sc-221978 sc-221978B sc-221978C sc-221978D | 5 mg 10 mg 25 mg 50 mg 100 mg | $188.00 $281.00 $555.00 $926.00 $1509.00 | ||
N-Acetyl-2,3-dehydro-2-deoxyneuraminic Acid, Sodium Salt exhibits distinctive characteristics as a neuraminidase by engaging in specific interactions with sialic acid residues on glycoproteins. Its structural conformation enables efficient substrate recognition, enhancing catalytic efficiency. The compound's unique binding dynamics influence the enzyme's active site, resulting in altered reaction kinetics and substrate specificity, which can significantly impact glycan remodeling processes in biological systems. | ||||||
Oseltamivir phosphate | 204255-11-8 | sc-208135 sc-208135A | 10 mg 200 mg | $179.00 $650.00 | 5 | |
Oseltamivir phosphate functions as a neuraminidase inhibitor, characterized by its ability to mimic sialic acid, allowing it to bind effectively to the enzyme's active site. This competitive inhibition alters the enzyme's catalytic pathway, leading to a decrease in the cleavage of sialic acid from glycoproteins. The compound's unique stereochemistry and electronic properties facilitate strong interactions with the enzyme, influencing its overall activity and stability in biochemical environments. | ||||||
Laninamivir-d3 | 203120-17-6 (unlabeled) | sc-280898 | 250 µg | $430.00 | ||
Laninamivir-d3 acts as a neuraminidase inhibitor by forming stable interactions with the enzyme's active site, disrupting its normal function. Its unique structural features enhance binding affinity, promoting a conformational change in the enzyme that impedes substrate access. The compound's distinct isotopic labeling allows for advanced tracking in biochemical assays, providing insights into enzyme kinetics and dynamics. This specificity in molecular interactions contributes to its effectiveness in modulating enzymatic activity. | ||||||
Zanamivir | 139110-80-8 | sc-208495 | 1 mg | $270.00 | 6 | |
Zanamivir functions as a neuraminidase inhibitor through its unique ability to mimic sialic acid, allowing it to effectively occupy the enzyme's active site. This competitive inhibition alters the enzyme's conformation, reducing its catalytic efficiency. The compound's rigid bicyclic structure enhances its binding stability, while its polar functional groups facilitate hydrogen bonding, further strengthening interactions with the enzyme. These characteristics influence the reaction kinetics, leading to a significant decrease in enzymatic activity. | ||||||
Laninamivir | 203120-17-6 | sc-488700 sc-488700A sc-488700B sc-488700C sc-488700D sc-488700E | 500 µg 5 mg 50 mg 100 mg 250 mg 1 g | $411.00 $2710.00 $18212.00 $27417.00 $41101.00 $70752.00 | ||
Laninamivir acts as a neuraminidase inhibitor by engaging in specific interactions with the enzyme's active site, where its elongated structure allows for optimal fit and binding. The presence of multiple functional groups enhances its solubility and promotes electrostatic interactions, which stabilize the enzyme-inhibitor complex. This results in a notable alteration of the enzyme's dynamics, effectively slowing down the reaction rate and impacting the overall enzymatic function. | ||||||
Zanamivir-13C,15N2 | sc-220399 | 250 µg | $490.00 | |||
Zanamivir-13C,15N2 exhibits unique characteristics as a neuraminidase by forming strong hydrogen bonds with key residues in the enzyme's active site. Its isotopic labeling with carbon and nitrogen enhances the precision of kinetic studies, allowing for detailed insights into reaction mechanisms. The compound's rigid conformation restricts conformational flexibility, leading to a significant decrease in enzymatic activity and altering substrate binding dynamics, thereby influencing the overall catalytic efficiency. | ||||||