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    Metal self-assembly mimosine peptides with enhanced antimicrobial activity: towards a new generation of multitasking chelating agents.

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    Type
    Article
    Authors
    Lachowicz, Joanna Izabela Izabela
    Dalla Torre, Gabriele
    Cappai, Rosita
    Randaccio, Enrico
    Nurchi, Valeria Marina
    Bachor, Remigiusz RB
    Szewczuk, Zbigniew
    Jaremko, Lukasz cc
    Jaremko, Mariusz cc
    Pisano, Maria Barbara MBP
    Cosentino, Sofia SC
    Orrù, Germano
    Ibba, Antonella AI
    Mujika, Joni JM
    Lopez, Xabier
    KAUST Department
    Biological and Environmental Sciences and Engineering (BESE) Division
    Bioscience Program
    Date
    2020
    Embargo End Date
    2021-01-28
    Submitted Date
    2019-11-26
    Permanent link to this record
    http://hdl.handle.net/10754/661514
    
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    Abstract
    Mimosine is a non-protein aminoacid with various properties, such as antibacterial, anti-inflammatory, anti-cancer and anti-virus among others. Due to its structure similarity with deferiprone (DFP), mimosine is a potential excellent metal chelator. In the present work, we combine experimental and theoretical (DFT) approaches in order to investigate the properties of mimosine peptides. Six different peptides were synthesized and their complex stoichiometry and stability were characterized by means of UV-Vis spectrophotometry. Then, the binding mode and self-assembly features of the peptides were evaluated using a DFT approach, taking into account different number of mimosine amino acids and varying the length of the spacer between the mimosine residues, finding a good agreement between experimental data and computational calculations. Further elucidations of the structural properties of these peptides allowed us to propose improvements in the structure of the mimosine moiety that can lead to enhanced affinity for high-valent metals. Moreover, we demonstrate that these peptides show an anti-microbial activity against gram positive bacteria that is enhanced by the formation of a complex with iron(III) ions. The mimosine peptides could be an alternative to Antimicrobial peptides (AMPs), which are expensive and susceptible to proteolytic degradation. In summary, in the present work, we propose a new generation of multipurpose mimosine-based peptides as a new metal self-assembly chelators that could be a corner point in biomedical and nanotechnological applications.
    Citation
    Lachowicz, J. I. I., Dalla Torre, G., Cappai, R., Randaccio, E., Nurchi, V. M., Bachor, R. R., … Lopez, X. (2020). Metal self-assembly mimosine peptides with enhanced antimicrobial activity: towards a new generation of multitasking chelating agents. Dalton Transactions. doi:10.1039/c9dt04545g
    Sponsors
    This work was supported by a grant No. UMO-2015/17/D/ST5/01329 from the National Science Centre, Poland. This work was also supported by Grants PGC2018-099321-B-I00 from the Ministry of Science and Universities through the Office of Science Research (MINECO/FEDER), and Grant IT588-13 from the Basque Government.
    Publisher
    Royal Society of Chemistry (RSC)
    Journal
    Dalton Transactions
    DOI
    10.1039/c9dt04545g
    Additional Links
    http://pubs.rsc.org/en/Content/ArticleLanding/2020/DT/C9DT04545G
    ae974a485f413a2113503eed53cd6c53
    10.1039/c9dt04545g
    Scopus Count
    Collections
    Articles; Biological and Environmental Science and Engineering (BESE) Division; Bioscience Program

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