Emergent antibacterial activity of<i>N</i>-(thiazol-2-yl)benzenesulfonamides in conjunction with cell-penetrating octaarginine

Ratrey, Poonam; Mahapatra, Amarjyoti Das; Pandit, Shiny; Hadianawala, Murtuza; Majhi, Sasmita; Mishra, Abhijit; Datta, Bhaskar

doi:10.1039/d1ra03882f

Cited by 3 publications

(6 citation statements)

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“…coli tested, ATCC 25922 and K12 (data not shown in this paper). This strain-selective activity is consistent with other thiazolyl benzenesulfonamide derivatives synthesized and tested in our lab . Intriguingly, even micromolar quantities of the BTB–R8 complex do not display antibacterial activity against E.…”

Section: Resultssupporting

confidence: 88%

“…The thiazole moiety has also been featured as a prominent motif that exerts antibacterial activity. , We recently incorporated the benzenesulfonamide and thiazole moieties into a single scaffold in the form of novel N-substituted (thiazol-2-yl)benzenesulfonamide derivatives and identified emergent antibacterial properties in conjunction with the cell-penetrating peptide (CPP) octaarginine . The antibacterial effect exerted by sulfonamides has been most commonly attributed to the inhibition of synthesis of nucleic acid precursors, thereby arresting growth and reproduction.…”

Section: Introductionmentioning

confidence: 99%

“…Our previous efforts established the broad functional scope of N-substituted (thiazol-2-yl)benzenesulfonamides complexed with CPP octaargininine (R8) . Notably, the complexes behaved differently as compared with the sum of individual effects of their components.…”

Section: Introductionmentioning

confidence: 99%

“…19,20 We recently incorporated the benzenesulfonamide and thiazole moieties into a single scaffold in the form of novel N-substituted (thiazol-2-yl)benzenesulfonamide derivatives and identified emergent antibacterial properties in conjunction with the cell-penetrating peptide (CPP) octaarginine. 21 The antibacterial effect exerted by sulfonamides has been most commonly attributed to the inhibition of synthesis of nucleic acid precursors, thereby arresting growth and reproduction. Other specific targets of sulfonamides include dihydropteroate synthase (DHPS), dihydrofolate reductase (DHFR), and carbonic anhydrases.…”

Section: Introductionmentioning

confidence: 99%

“…30−32 Our previous efforts established the broad functional scope of N-substituted (thiazol-2-yl)benzenesulfonamides complexed with CPP octaargininine (R8). 21 Notably, the complexes behaved differently as compared with the sum of individual effects of their components. In the absence of complexation with R8, the derivatives displayed antibacterial behavior in organic solvents but not in aqueous solutions.…”

Section: Introductionmentioning

confidence: 99%

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Intracellular Bacterial Targeting by a Thiazolyl Benzenesulfonamide and Octaarginine Peptide Complex

Ratrey

Datta

Mishra

2022

ACS Appl. Bio Mater.

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A brominated thiazolyl benzenesulfonamide (BTB) derivative is conjugated with the cell-penetrating peptide octaarginine (R8) in an effort to construct innovative antibacterial products. The noncovalent complex of BTB and R8 is characterized by Fourier transform infrared (FTIR) spectroscopy, which indicates hydrogen bonding between the two constituents. Attachment of the peptide moiety renders aqueous solubility to the hydrophobic benzenesulfonamide drug and bestows bactericidal activity. Confocal imaging in conjunction with dye probes shows successful clearance of intracellular Staphylococcus aureus bacteria by the BTB–R8 complex. Scanning electron micrographs and studies with a set of fluorescent dyes suggest active disruption of the bacterial cell membrane by the BTB–R8 complex. In contrast, the complex of BTB with octalysine (K8) fails to cause membrane damage and displays a modest antibacterial effect. A complex of BTB with the water-soluble hydrophilic polymer poly(vinylpyrrolidone) (PVP) does not display any antibacterial effect, indicating the distinctive role of the cell-penetrating peptide (CPP) R8 in the cognate complex. The leakage of the encapsulated dye from giant unilamellar vesicles upon interaction with the BTB–R8 complex further highlights the membrane activity of the complex, which cannot be accomplished by bare sulfonamide alone. This work broadens the scope of use of CPPs with respect to eliciting antibacterial activity and potentially expands the limited arsenal of membrane-targeting antibiotics.

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Section: Resultssupporting

confidence: 88%