Thiophene Sulfonamides
Thiophene Sulfonamides - Related Videos
01:23
Amines to Sulfonamides: The Hinsberg Test
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2023
The Hinsberg test is a method to identify primary, secondary and tertiary amines, named after its pioneer, Oscar Hinsberg. Here, amines are treated with benzenesulfonyl chloride, also known as the Hinsberg reagent, in the presence of an excess of aqueous base, followed by acidification. Based on the nature of the amines, different changes are observed. Generally, a primary amine reacts with the Hinsberg reagent to produce an N-substituted benzenesulfonamide. The electron-withdrawing sulfonyl...
10:42
Preparation of N-(2-alkoxyvinyl)sulfonamides from N-tosyl-1,2,3-triazoles and Subsequent Conversion to Substituted Phthalans and Phenethylamines
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2018
Representative experimental procedures for the synthesis of N-(2-alkoxyvinyl)sulfonamides and subsequent conversion to phthalan and phenethylamine derivatives are presented in detail.
03:38
hFTAA Staining of Amyloid Deposits: A Technique to Visualize Amyloid Fibrils Using Oligothiophene-Based Dye for Fluorescence Imaging in Tissue Sections
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2025
This video describes a technique to stain amyloids in tissue sections using a luminescent-conjugated oligothiophene dye - heptamer-formyl thiophene acetic acid, or hFTAA - for fluorescence imaging. Amyloids are β-sheet-rich abnormal protein aggregates. Their detection in tissue samples is helpful in the diagnosis and treatment of amyloid-associated diseases or proteinopathies.
03:26
Analyzing Amyloid Structures in a Tissue Section Using Fluorescence Lifetime Imaging Microscopy
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2025
Source: Nyström, S., et al., Imaging Amyloid Tissues Stained with Luminescent Conjugated Oligothiophenes by Hyperspectral Confocal Microscopy and Fluorescence Lifetime Imaging. J. Vis. Exp. (2017).This video demonstrates analyzing amyloid structures with fluorescence lifetime imaging microscopy or FLIM, using hFTAA dye to reveal compact cores as blue/green and unstable peripheries as red/yellow in color-coded images, reflecting amyloid organization.
08:11
Failure Analysis of Batteries Using Synchrotron-based Hard X-ray Microtomography
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Cited by 7 •
2015
Synchrotron-based hard X-ray microtomography is used to image the electrochemical growth of dendrites from a lithium metal electrode through a solid polymer electrolyte membrane.
FAQs
Binding depends on the combined contribution of two chemically different regions. The thiophene ring can support hydrophobic and aromatic contacts, while the sulfonamide group can provide hydrogen-bonding interactions and, in some chemical environments, ionic contacts. This complementary interaction pattern can help position a compound within a protein site and influence its biological activity.
Substituents on the thiophene ring or sulfonamide region can alter several properties at once, including potency, selectivity, solubility, and metabolic stability. These changes affect how effectively a compound interacts with a protein and how suitable it may be for biological investigation. Comparing strategically modified derivatives therefore helps connect chemical structure with observed activity.
The two regions contribute different interaction capabilities rather than serving identical structural roles. The aromatic thiophene ring can favor hydrophobic or aromatic contacts, whereas the sulfonamide group can participate in hydrogen bonding and potentially ionic interactions. Modifying either region may therefore change binding behavior, while preserving the scaffold's ability to engage complementary features in a protein site.
Researchers can examine a series of compounds that vary in substituents on the thiophene ring, the sulfonamide group, or both. Comparing their potency, selectivity, solubility, and metabolic stability reveals how specific structural changes influence biological performance. This structure-focused approach supports the identification of derivatives with more favorable combinations of activity and chemical properties.
In enzyme inhibitor studies, these compounds can serve as adaptable molecular scaffolds for examining how chemical features affect protein binding and activity. Differences among derivatives may help researchers evaluate potency and selectivity while relating those outcomes to hydrogen bonding, aromatic contacts, hydrophobic interactions, or ionic interactions. Such comparisons can contribute to understanding enzyme function and inhibitor design.
Their research relevance extends beyond enzyme inhibition. Thiophene sulfonamides can support investigations of protein function and the design of potential agents with antimicrobial, anti-inflammatory, or anticancer activity. In each context, researchers can use structural variation to explore biological effects while also considering properties such as selectivity, solubility, and metabolic stability.