Introduction of a β-leucine residue instead of leucine9 and glycine10 residues in Temporin L for improved cell selectivity, stability and activity against planktonic and biofilm of methicillin resistant S. aureus
[Display omitted] •L9βl-TL showed higher proteolytic stability, therapeutic index and activity against MRSA biofilm than Temporin-L (TL).•Though unordered in bacterial membrane-mimetic lipid vesicles, L9βl-TL depolarized these vesicles and live MRSA.•The results show the design of a TL-analogue with...
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Published in | Bioorganic chemistry Vol. 134; p. 106440 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
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Elsevier Inc
01.05.2023
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Abstract | [Display omitted]
•L9βl-TL showed higher proteolytic stability, therapeutic index and activity against MRSA biofilm than Temporin-L (TL).•Though unordered in bacterial membrane-mimetic lipid vesicles, L9βl-TL depolarized these vesicles and live MRSA.•The results show the design of a TL-analogue with higher therapeutic potential by impairing its secondary structure.
Leucine and glycine residues, at the 9th and 10th positions of helical domain of naturally occurring antimicrobial peptide (AMP), Temporin L were substituted with an unnatural amino acid, β-leucine (homovaline) to improve its serum protease stability, haemolytic/cytotoxic properties and reduce the size to some extent. The designed analogue, L9βl-TL showed either equal or improved antimicrobial activity to TL against different microorganisms including the resistant strains. Interestingly, L9βl-TL also exhibited lower haemolytic and cytotoxic activities against human red blood cells and 3T3 cells, respectively. Moreover, L9βl-TL showed antibacterial activity in presence of 25% (v/v) human serum and showed resistance against proteolytic cleavage in presence of it that suggested the serum protease stability of the TL-analogue. L9βl-TL exhibited un-ordered secondary structures in both bacterial and mammalian membrane mimetic lipid vesicles as compared to the helical structures of TL in these environments. However, tryptophan fluorescence studies demonstrated more selective interaction of L9βl-TL with bacterial membrane mimetic lipid vesicles in comparison to non-selective interactions of TL with both kinds of lipid vesicles. Membrane depolarization studies with live MRSA and bacterial membrane-mimetic lipid vesicles suggested a membrane-disrupting mode of action of L9βl-TL. L9βl-TL showed faster bactericidal mechanism compared to TL against MRSA. Interestingly, L9βl-TL was found as more potent than TL either in inhibiting biofilm formation or in eradicating the mature biofilm formed by MRSA. Overall, the present work demonstrates a simple and useful strategy to design of an analogue of TL, with minimal modifications while maintaining its antimicrobial activity with lesser toxicity and higher stability which could be attempted for other AMPs as well. |
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AbstractList | [Display omitted]
•L9βl-TL showed higher proteolytic stability, therapeutic index and activity against MRSA biofilm than Temporin-L (TL).•Though unordered in bacterial membrane-mimetic lipid vesicles, L9βl-TL depolarized these vesicles and live MRSA.•The results show the design of a TL-analogue with higher therapeutic potential by impairing its secondary structure.
Leucine and glycine residues, at the 9th and 10th positions of helical domain of naturally occurring antimicrobial peptide (AMP), Temporin L were substituted with an unnatural amino acid, β-leucine (homovaline) to improve its serum protease stability, haemolytic/cytotoxic properties and reduce the size to some extent. The designed analogue, L9βl-TL showed either equal or improved antimicrobial activity to TL against different microorganisms including the resistant strains. Interestingly, L9βl-TL also exhibited lower haemolytic and cytotoxic activities against human red blood cells and 3T3 cells, respectively. Moreover, L9βl-TL showed antibacterial activity in presence of 25% (v/v) human serum and showed resistance against proteolytic cleavage in presence of it that suggested the serum protease stability of the TL-analogue. L9βl-TL exhibited un-ordered secondary structures in both bacterial and mammalian membrane mimetic lipid vesicles as compared to the helical structures of TL in these environments. However, tryptophan fluorescence studies demonstrated more selective interaction of L9βl-TL with bacterial membrane mimetic lipid vesicles in comparison to non-selective interactions of TL with both kinds of lipid vesicles. Membrane depolarization studies with live MRSA and bacterial membrane-mimetic lipid vesicles suggested a membrane-disrupting mode of action of L9βl-TL. L9βl-TL showed faster bactericidal mechanism compared to TL against MRSA. Interestingly, L9βl-TL was found as more potent than TL either in inhibiting biofilm formation or in eradicating the mature biofilm formed by MRSA. Overall, the present work demonstrates a simple and useful strategy to design of an analogue of TL, with minimal modifications while maintaining its antimicrobial activity with lesser toxicity and higher stability which could be attempted for other AMPs as well. |
ArticleNumber | 106440 |
Author | Dewangan, Rikeshwer Prasad Verma, Neeraj Kumar Harioudh, Munesh Kumar Ghosh, Jimut Kanti |
Author_xml | – sequence: 1 givenname: Neeraj Kumar surname: Verma fullname: Verma, Neeraj Kumar – sequence: 2 givenname: Rikeshwer Prasad surname: Dewangan fullname: Dewangan, Rikeshwer Prasad email: rpdewangan@jamiahamdard.ac.in – sequence: 3 givenname: Munesh Kumar surname: Harioudh fullname: Harioudh, Munesh Kumar – sequence: 4 givenname: Jimut Kanti surname: Ghosh fullname: Ghosh, Jimut Kanti email: jk_ghosh@cdri.res.in |
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Keywords | DiSC3 PC AMP MRSA PG TL Fmoc Temporin L Methicillin resistant S. aureus β-leucine MRSA biofilm Antimicrobial peptide |
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•L9βl-TL showed higher proteolytic stability, therapeutic index and activity against MRSA biofilm than Temporin-L (TL).•Though unordered in... |
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SubjectTerms | Antimicrobial peptide Methicillin resistant S. aureus MRSA biofilm Temporin L β-leucine |
Title | Introduction of a β-leucine residue instead of leucine9 and glycine10 residues in Temporin L for improved cell selectivity, stability and activity against planktonic and biofilm of methicillin resistant S. aureus |
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