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dc.contributor.authorLachowicz, Joanna Izabela Izabela
dc.contributor.authorDalla Torre, Gabriele
dc.contributor.authorCappai, Rosita
dc.contributor.authorRandaccio, Enrico
dc.contributor.authorNurchi, Valeria Marina
dc.contributor.authorBachor, Remigiusz RB
dc.contributor.authorSzewczuk, Zbigniew
dc.contributor.authorJaremko, Lukasz
dc.contributor.authorJaremko, Mariusz
dc.contributor.authorPisano, Maria Barbara MBP
dc.contributor.authorCosentino, Sofia SC
dc.contributor.authorOrrù, Germano
dc.contributor.authorIbba, Antonella AI
dc.contributor.authorMujika, Joni JM
dc.contributor.authorLopez, Xabier
dc.date.accessioned2020-02-13T11:05:00Z
dc.date.available2020-02-13T11:05:00Z
dc.date.issued2020
dc.date.submitted2019-11-26
dc.identifier.citationLachowicz, 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
dc.identifier.doi10.1039/c9dt04545g
dc.identifier.urihttp://hdl.handle.net/10754/661514
dc.description.abstractMimosine 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.
dc.description.sponsorshipThis 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.
dc.publisherRoyal Society of Chemistry (RSC)
dc.relation.urlhttp://pubs.rsc.org/en/Content/ArticleLanding/2020/DT/C9DT04545G
dc.rightsArchived with thanks to Dalton Transactions
dc.titleMetal self-assembly mimosine peptides with enhanced antimicrobial activity: towards a new generation of multitasking chelating agents.
dc.typeArticle
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Division
dc.contributor.departmentBioscience Program
dc.identifier.journalDalton Transactions
dc.rights.embargodate2021-01-28
dc.eprint.versionPost-print
dc.contributor.institutionDepartment of Medical Sciences and Public Health, University of Cagliari, Cittadella Universitaria, 09042 Monserrato, Italy
dc.contributor.institutionKimika Fakultatea, Euskal Herriko Unibertsitatea UPV/EHU, Donostia International Physics Center (DIPC), P.K. 1072, Donostia, Euskadi, 20080 San Sebastian, Spain
dc.contributor.institutionUCIBIO/REQUIMTE, Departamento de Química e Bioquímica, Faculdade de Ciências, Universidade do Porto, Rua do Campo Alegre, s/n, 4169-007 Porto, Portugal.
dc.contributor.institutionDepartment of Life Sciences, University of Cagliari, Cittadella Universitaria, 09042 Monserrato, Italy
dc.contributor.institutionFaculty of Chemistry, University of Wrocław, F. Joliot-Curie 14, 50-383 Wrocław, Poland
dc.contributor.institutionDepartment of Surgical Sciences, University of Cagliari, Cittadella Universitaria, 09042 Monserrato, Italy
kaust.personJaremko, Lukasz
kaust.personJaremko, Mariusz
dc.date.accepted2020-01-27
refterms.dateFOA2020-02-13T11:05:46Z


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