ArticleAntimicrobial agents and chemotherapy2016
The Disulfide Bond of the Peptide Thanatin Is Dispensible for Its Antimicrobial Activity In Vivo and In Vitro.
Article in Antimicrobial agents and chemotherapy, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 44 citations in OpenAlex.
- α-Bromocinnamaldehyde combats ESKAPE pathogens through dual bactericidal mechanism.Folia microbiologica · 2025Article
- An engineered redox-switchable streptavidin mutein enables the high-affinity capture and efficient elution of biotinylated ligands.Protein science : a publication of the Protein Society · 2025Article
- Fighting Antimicrobial Resistance: Innovative Drugs in Antibacterial Research.Angewandte Chemie (International ed. in English) · 2025Review
- Single Disulfide Bond in Host Defense Thanatin Analog Peptides: Antimicrobial Activity, Atomic-Resolution Structures and Target Interactions.International journal of molecular sciences · 2024Article
- Innovative Strategies and Methodologies in Antimicrobial Peptide Design.Journal of functional biomaterials · 2024Review
- Thanatin: A Promising Antimicrobial Peptide Targeting the Achilles' Heel of Multidrug-Resistant Bacteria.International journal of molecular sciences · 2024Review
- Thanatin and vinyl sulfide analogues as narrow spectrum antimicrobial peptides that synergise with polymyxin B.Frontiers in pharmacology · 2024Article
- Discovery, characterization, and redesign of potent antimicrobial thanatin orthologs fromJournal of structural biology: X · 2023Article
- Quaternary Ammonium Salts of Cationic Lipopeptides with Lysine Residues - Synthesis, Antimicrobial, Hemolytic and Cytotoxic Activities.Probiotics and antimicrobial proteins · 2023Article
- Enhanced Antibacterial Activity of Substituted Derivatives of NCR169C Peptide.International journal of molecular sciences · 2023Article
- Making a chink in their armor: Current and next-generation antimicrobial strategies against the bacterial cell envelope.Advances in microbial physiology · 2023Article
- Current Promising Strategies against Antibiotic-Resistant Bacterial Infections.Antibiotics (Basel, Switzerland) · 2022Review
- Secondary Structural Transformation of Bovine Lactoferricin Affects Its Antibacterial Activity.Probiotics and antimicrobial proteins · 2021Article
- Thanatin: An Emerging Host Defense Antimicrobial Peptide with Multiple Modes of Action.International journal of molecular sciences · 2021Review
- Contemporaneous Measurement of Outer and Inner Membrane Permeability in Gram-negative Bacteria.Bio-protocol · 2020Article
- Expression of Thanatin in HEK293 Cells and Investigation of its Antibacterial Effects on Some Human Pathogens.Protein and peptide letters · 2020Article
- Calcium-siRNA Nanocomplexes Optimized by Bovine Serum Albumin Coating Can Achieve Convenient and Efficient siRNA Delivery for Periodontitis Therapy.International journal of nanomedicine · 2020Article
- Repurposing Ellipticine Hydrochloride to Combat Colistin-Resistant Extraintestinal PathogenicFrontiers in microbiology · 2020Article
- The antimicrobial peptide thanatin disrupts the bacterial outer membrane and inactivates the NDM-1 metallo-β-lactamase.Nature communications · 2019Article
- The Synergism of the Small Molecule ENOblock and Fluconazole Against Fluconazole-ResistantFrontiers in microbiology · 2019Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Thanatin (THA) displays potent antibiotic activity, especially against extended-spectrum-β-lactamase (ESBL)-producing Escherichia coli both in vitro and in vivo, with minimal hemolytic toxicity and satisfactory stability in plasma. However, the high cost of thanatin significantly limits its development and clinical application. To reduce the cost of peptide synthesis, a formulation of cyclic thanatin (C-thanatin) called linear thanatin (L-thanatin) was synthesized and its activity was evaluated in vivo and in vitro Results showed that C-thanatin and L-thanatin MICs did not differ against eight Gram-negative and two Gram-positive bacterial strains. Furthermore, the survival rates of ESBL-producing-E. coli-infected mice were consistent after C-thanatin or L-thanatin treatment at 5 or 10 mg/kg of body weight. Neither C-thanatin nor L-thanatin showed toxicity for human red blood cells (hRBCs) and human umbilical vein endothelial cells (HUVECs) at a concentration as high as 256 μg/ml. Results of circular dichroism spectroscopy indicated that the secondary structure of L-thanatin is extremely similar to that of C-thanatin. Membrane permeabilization and depolarization assays showed that C-thanatin and L-thanatin have similar abilities to permeabilize the outer and inner membranes and to induce membrane depolarization in ESBL-producing E. coli However, neither of them caused significant HUVEC membrane permeability. These findings indicate that the two peptides have similar effects on bacterial cell membranes and that the disulfide bond in thanatin is not essential for its antimicrobial activities in vivo and in vitro L-thanatin is thus a promising low-cost peptide candidate for treating ESBL-producing E. coli infections.
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