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Antimicrobial peptide induced colloidal transformations in bacteria-mimetic vesicles: combining in silico tools and experimental methods
Department of Chemistry, University of Fribourg, Chemin Du Musée 9, 1700 Fribourg, Switzerland.
Department of Fundamental Chemistry, Federal University of Pernambuco, Cidade Universitária, 50740-560 Recife, Brazil.
Department of Fundamental Chemistry, Federal University of Pernambuco, Cidade Universitária, 50740-560 Recife, Brazil.
Umeå University, Faculty of Science and Technology, Department of Chemistry. Umeå University, Faculty of Medicine, Umeå Centre for Microbial Research (UCMR).ORCID iD: 0000-0003-2646-8501
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2021 (English)In: Journal of Colloid and Interface Science, ISSN 0021-9797, E-ISSN 1095-7103, Vol. 596, p. 352-363Article in journal (Refereed) Published
Abstract [en]

With the growing challenges of bacteria becoming resistant to conventional antibiotics, antimicrobial peptides (AMPs) may offer a potential alternative. One of the most studied AMPs, the human cathelicidin derived AMP LL-37 is notable for its antimicrobial activity even though its mechanism of action is not fully understood yet. This work investigates the interaction of LL-37 with 1-Palmitoyl-2-oleoyl-sn-glycero-3-phospho-rac-(1-glycerol) (POPG) vesicles, which were employed as a bacterial membrane model given the common presence of this phospholipid in the bacterial membrane. Experimental techniques including small angle X-ray scattering, transmission electron microscopy and dynamic light scattering were used to characterize the interactions among LL-37 and POPG. Molecular dynamics simulations complement the experimental studies with molecular-level insights into the process. LL-37 was discovered to actively and critically interact with the POPG vesicles, modifying the membrane curvature that eventually leads to structural transformations from vesicles to mixed micelles. The results shed light on the mechanisms underlying the interactions among LL-37 and bacteria mimetic vesicles and can guide the further development of AMP based antimicrobial materials and therapies.

Place, publisher, year, edition, pages
Elsevier, 2021. Vol. 596, p. 352-363
Keywords [en]
Vesicles, Antimicrobial peptides, POPG, LL-37, Self-assembly, SAXS, Cryo-TEM, Coarse-grain molecular dynamics simulations
National Category
Physical Chemistry Biophysics Theoretical Chemistry Other Basic Medicine Condensed Matter Physics
Identifiers
URN: urn:nbn:se:umu:diva-182119DOI: 10.1016/j.jcis.2021.03.060ISI: 000645901500005Scopus ID: 2-s2.0-85103796398OAI: oai:DiVA.org:umu-182119DiVA, id: diva2:1542947
Available from: 2021-04-09 Created: 2021-04-09 Last updated: 2023-09-05Bibliographically approved

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Ramstedt, MadeleineSandblad, Linda

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