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  1. Article ; Online: DP1, a multifaceted synthetic peptide: Mechanism of action, activity and clinical potential.

    Maan, Mayank / Goyal, Hemant / Joshi, Shubhi / Barman, Panchali / Sharma, Sheetal / Kumar, Rajesh / Saini, Avneet

    Life sciences

    2024  Volume 340, Page(s) 122458

    Abstract: Aims: Microbial infections remain a leading cause of mortality worldwide, with Staphylococcus aureus (S. aureus) being a prominent etiological agent, responsible for causing persistent bacterial infections in humans. It is a nosocomial, opportunistic ... ...

    Abstract Aims: Microbial infections remain a leading cause of mortality worldwide, with Staphylococcus aureus (S. aureus) being a prominent etiological agent, responsible for causing persistent bacterial infections in humans. It is a nosocomial, opportunistic pathogen, capable to propagate within the bloodstream and withstand therapeutic interventions. In the current study, a novel, indigenously designed synthetic antimicrobial peptide (sAMP) has been evaluated for its antimicrobial potential to inhibit the growth and proliferation of S. aureus.
    Main methods: The sAMP, designed peptide (DP1) was evaluated for its minimum inhibitory concentration (MIC) and minimum bactericidal concentration (MBC) against a panel of pathogenic bacterial strains. Membrane mechanistic studies were performed by measuring membrane conductivity via dielectric spectroscopy and visualizing changes in bacterial membrane structure through field emission scanning electron microscopy (FE-SEM). Further, DP1 was tested for its in vivo antimicrobial potential in an S. aureus-induced systemic infection model.
    Key findings: The results indicated that DP1 has the potential to inhibit the growth and proliferation of a broad spectrum of Gram-positive, Gram-negative and multidrug-resistant (MDR) bacterial strains. Strong bactericidal effect attributed to change in electrical conductivity of the bacterial cells leading to membrane disruption was observed through dielectric spectroscopy and FE-SEM micrographs. Further, in the in vivo murine systemic infection study, 50 % reduction in S. aureus bioburden was observed within 1 day of the administration of DP1.
    Significance: The results indicate that DP1 is a multifaceted peptide with potent bactericidal, antioxidant and therapeutic properties. It holds significance as a novel drug candidate to effectively combat S. aureus-mediated systemic infections.
    MeSH term(s) Humans ; Animals ; Mice ; Staphylococcus aureus ; Anti-Bacterial Agents/pharmacology ; Anti-Bacterial Agents/chemistry ; Peptides/pharmacology ; Anti-Infective Agents/pharmacology ; Staphylococcal Infections/drug therapy ; Staphylococcal Infections/microbiology ; Bacteria ; Microbial Sensitivity Tests ; Phenylmercury Compounds
    Chemical Substances 4-(4-sulfophenylazo)-2-mercuriphenol (69630-03-1) ; Anti-Bacterial Agents ; Peptides ; Anti-Infective Agents ; Phenylmercury Compounds
    Language English
    Publishing date 2024-01-23
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 3378-9
    ISSN 1879-0631 ; 0024-3205
    ISSN (online) 1879-0631
    ISSN 0024-3205
    DOI 10.1016/j.lfs.2024.122458
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: In Vivo Acute Toxicity and Therapeutic Potential of a Synthetic Peptide, DP1 in a Staphylococcus aureus Infected Murine Wound Excision Model.

    Barman, Panchali / Sharma, Chakshu / Joshi, Shubhi / Sharma, Sheetal / Maan, Mayank / Rishi, Praveen / Singla, Neha / Saini, Avneet

    Probiotics and antimicrobial proteins

    2023  

    Abstract: Bacterial infections at the surgical sites are one of the most prevalent skin infections that impair the healing mechanism. They account for about 20% of all types of infections and lead to approximately 75% of surgical-site infection-associated ... ...

    Abstract Bacterial infections at the surgical sites are one of the most prevalent skin infections that impair the healing mechanism. They account for about 20% of all types of infections and lead to approximately 75% of surgical-site infection-associated mortality. Several antibiotics, such as cephalosporins, fluoroquinolones, quinolones, penicillin, sulfonamides, etc., that are used to treat such wound infections not only counter infections but also disrupt the normal flora. Moreover, antibiotics, when used for a prolonged duration, may impair the formation of new blood vessels, delay collagen production, or inhibit the migration of certain cells involved in wound repair, leading to an impaired healing process. Therefore, there is a dire need for alternate therapeutic approaches against such infections. Antimicrobial peptides have gained considerable attention as a promising strategy to counter these pathogens and prevent the spread of infection. Recently, we have reported a designed peptide, DP1, and its broad-spectrum in vitro antimicrobial activity against Gram-positive and Gram-negative bacteria. In the present study, in vivo acute toxicity of DP1 was evaluated and even at a high dose (20 mg/kg body weight) of DP1, a 100% survival of mice was observed. Subsequently, a Staphylococcus aureus-infected murine wound excision model was established to assess the wound healing efficacy of DP1. The study revealed significant wound healing vis-a-vis attenuated S. aureus bioburden at the wound site and also controlled the oxidative stress depicting anti-oxidant activity as well. Healing of the infected wounds was also verified by histopathological examination. Based on the results of this study, it can be concluded that DP1 improves wound resolution despite infections and promotes the healing mechanism. Hence, DP1 holds compelling potential as a novel antimicrobial drug that requires further explorations in clinical platforms.
    Language English
    Publishing date 2023-11-01
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2487792-X
    ISSN 1867-1314 ; 1867-1306
    ISSN (online) 1867-1314
    ISSN 1867-1306
    DOI 10.1007/s12602-023-10176-1
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Design, characterization and structure-function analysis of novel antimicrobial peptides based on the N-terminal CATH-2 fragment.

    Sharma, Pratibha / Sharma, Sheetal / Joshi, Shubhi / Barman, Panchali / Bhatt, Aashish / Maan, Mayank / Singla, Neha / Rishi, Praveen / Ali, Md Ehesan / Preet, Simran / Saini, Avneet

    Scientific reports

    2022  Volume 12, Issue 1, Page(s) 12058

    Abstract: The emergence of multidrug resistance coupled with shrinking antibiotic pipelines has increased the demand of antimicrobials with novel mechanisms of action. Therefore, researchers across the globe are striving to develop new antimicrobial substances to ... ...

    Abstract The emergence of multidrug resistance coupled with shrinking antibiotic pipelines has increased the demand of antimicrobials with novel mechanisms of action. Therefore, researchers across the globe are striving to develop new antimicrobial substances to alleviate the pressure on conventional antibiotic therapies. Host-Defence Peptides (HDPs) and their derivatives are emerging as effective therapeutic agents against microbial resistance. In this study, five analogs (DP1-5) of the N-terminal (N-15) fragment of CATH-2 were designed based on the delicate balance between various physicochemical properties such as charge, aliphatic character, amphipathicity and hydrophobicity. By means of in-silico and in-vitro studies a novel peptide (DP1) with the sequence "RFGRFLRKILRFLKK" was found to be more effective and less toxic than the N-terminal CATH-2 peptide. Circular dichroism spectroscopy and differential scanning calorimetry were applied for structural insights. Antimicrobial, haemolytic, and cytotoxic activities were also assessed. The resulting peptide was characterized by low cytotoxicity, low haemolytic activity, and efficient anti-microbial activity. Structurally, it displayed strong helical properties irrespective of the solvent environment and was stable in membrane-mimicking environments. Taken together, the data suggests that DP1 can be explored as a promising therapeutic agent with possible clinical applications.
    MeSH term(s) Anti-Bacterial Agents/chemistry ; Anti-Infective Agents/chemistry ; Anti-Infective Agents/pharmacology ; Antimicrobial Cationic Peptides/chemistry ; Antimicrobial Cationic Peptides/pharmacology ; Antimicrobial Peptides ; Circular Dichroism ; Hemolysis ; Humans ; Microbial Sensitivity Tests
    Chemical Substances Anti-Bacterial Agents ; Anti-Infective Agents ; Antimicrobial Cationic Peptides ; Antimicrobial Peptides
    Language English
    Publishing date 2022-07-14
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-022-16303-2
    Database MEDical Literature Analysis and Retrieval System OnLINE

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