ORCID Profile
0000-0002-4124-7339
Current Organisation
Indian Institute of Science
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Publisher: Wiley
Date: 18-03-2008
Publisher: Royal Society of Chemistry (RSC)
Date: 2020
DOI: 10.1039/D0CC05653G
Abstract: We identified several CH–π donor–acceptor pairs involving amino acid side chains with less polarized C–H bonds at a solvent-exposed site between the strands of a β-hairpin peptide.
Publisher: Royal Society of Chemistry (RSC)
Date: 2020
DOI: 10.1039/D0SC03060K
Abstract: Amino acid residues adopt a right-handed α-helical conformation with increasing strength of the n → π* interaction. We also demonstrate a direct consequence of n → π* interactions on enhancing the structural stability of proteins.
Publisher: EMBO
Date: 11-05-2023
Abstract: The bacterial toxin CcdB (Controller of Cell death or ision B) targets DNA Gyrase, an essential bacterial topoisomerase, which is also the molecular target for fluoroquinolones. Here, we present a short cell‐penetrating 24‐mer peptide, CP1‐WT, derived from the Gyrase‐binding region of CcdB and examine its effect on growth of Escherichia coli , Salmonella Typhimurium, Staphylococcus aureus and a carbapenem‐ and tigecycline‐resistant strain of Acinetobacter baumannii in both axenic cultures and mouse models of infection. The CP1‐WT peptide shows significant improvement over ciprofloxacin in terms of its in vivo therapeutic efficacy in treating established infections of S. Typhimurium, S. aureus and A. baumannii . The molecular mechanism likely involves inhibition of Gyrase or Topoisomerase IV, depending on the strain used. The study validates the CcdB binding site on bacterial DNA Gyrase as a viable and alternative target to the fluoroquinolone binding site.
Publisher: Wiley
Date: 20-10-2021
Abstract: Amino acid side chains are key to fine‐tuning the microenvironment polarity in proteins composed of polar amide bonds. Here, we report that substituting an oxygen atom of the backbone amide bond with sulfur atom desolvates the thioamide bond, thereby increasing its lipophilicity. The impact of such local desolvation by O to S substitution in proteins was tested by synthesizing thioamidated variants of Pin1 WW domain. We observe that a thioamide acts in synergy with nonpolar amino acid side chains to reduce the microenvironment polarity and increase protein stability by more than 14 °C. Through favorable van der Waals and hydrogen bonding interactions, this single atom substitution significantly stabilizes proteins without altering the amino acid sequence and structure of the native protein.
Publisher: Elsevier
Date: 2021
Publisher: Royal Society of Chemistry (RSC)
Date: 2022
DOI: 10.1039/D1CB00229E
Abstract: NMR studies of macrocyclic β-hairpin model systems demonstrate that thioamides can be tolerated at both hydrogen bond donor and hydrogen bond acceptor positions.
Publisher: Royal Society of Chemistry (RSC)
Date: 2018
DOI: 10.1039/C7SC04671E
Abstract: Thioamide substitution into macrocyclic peptides increases the conformational rigidity of the backbone resulting in enhanced biological activity and metabolic stability.
Publisher: Wiley
Date: 22-03-2020
DOI: 10.1002/PSC.3248
Publisher: Springer New York
Date: 2009
Publisher: Springer Science and Business Media LLC
Date: 02-06-2022
DOI: 10.1038/S41589-022-01060-0
Abstract: Protein tertiary structure mimetics are valuable tools to target large protein–protein interaction interfaces. Here, we demonstrate a strategy for designing dimeric helix-hairpin motifs from a previously reported three-helix-bundle miniprotein that targets the receptor-binding domain (RBD) of severe acute respiratory syndrome-coronavirus-2 (SARS-CoV-2). Through truncation of the third helix and optimization of the interhelical loop residues of the miniprotein, we developed a thermostable dimeric helix-hairpin. The dimeric four-helix bundle competes with the human angiotensin-converting enzyme 2 (ACE2) in binding to RBD with 2:2 stoichiometry. Cryogenic-electron microscopy revealed the formation of dimeric spike ectodomain trimer by the four-helix bundle, where all the three RBDs from either spike protein are attached head-to-head in an open conformation, revealing a novel mechanism for virus neutralization. The proteomimetic protects hamsters from high dose viral challenge with replicative SARS-CoV-2 viruses, demonstrating the promise of this class of peptides that inhibit protein–protein interaction through target dimerization.
Publisher: Springer Science and Business Media LLC
Date: 28-09-2023
No related grants have been discovered for Jayanta Chatterjee.