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Antimicrobial pepti...
Antimicrobial peptide induced colloidal transformations in bacteria-mimetic vesicles : combining in silico tools and experimental methods
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- Freire, Rafael V.M. (författare)
- Department of Chemistry, University of Fribourg, Chemin Du Musée 9, 1700 Fribourg, Switzerland
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- Pillco-Valencia, Yeny (författare)
- Department of Fundamental Chemistry, Federal University of Pernambuco, Cidade Universitária, 50740-560 Recife, Brazil
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- da Hora, Gabriel C.A. (författare)
- Department of Fundamental Chemistry, Federal University of Pernambuco, Cidade Universitária, 50740-560 Recife, Brazil
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- Ramstedt, Madeleine (författare)
- Umeå universitet,Kemiska institutionen,Umeå Centre for Microbial Research (UCMR)
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- Sandblad, Linda (författare)
- Umeå universitet,Kemiska institutionen,Umeå Centre for Microbial Research (UCMR)
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- Soares, Thereza A. (författare)
- Department of Fundamental Chemistry, Federal University of Pernambuco, Cidade Universitária, 50740-560 Recife, Brazil
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- Salentinig, Stefan (författare)
- epartment of Chemistry, University of Fribourg, Chemin Du Musée 9, 1700 Fribourg, Switzerland
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(creator_code:org_t)
- Elsevier, 2021
- 2021
- Engelska.
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Ingår i: Journal of Colloid and Interface Science. - : Elsevier. - 0021-9797 .- 1095-7103. ; 596, s. 352-363
- Relaterad länk:
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https://doi.org/10.1...
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https://umu.diva-por... (primary) (Raw object)
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https://doi.org/10.1...
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Ämnesord
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- 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.
Ämnesord
- NATURVETENSKAP -- Kemi -- Fysikalisk kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences -- Physical Chemistry (hsv//eng)
- NATURVETENSKAP -- Biologi -- Biofysik (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biophysics (hsv//eng)
- NATURVETENSKAP -- Kemi -- Teoretisk kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences -- Theoretical Chemistry (hsv//eng)
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Andra medicinska och farmaceutiska grundvetenskaper (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Other Basic Medicine (hsv//eng)
- NATURVETENSKAP -- Fysik -- Den kondenserade materiens fysik (hsv//swe)
- NATURAL SCIENCES -- Physical Sciences -- Condensed Matter Physics (hsv//eng)
Nyckelord
- Vesicles
- Antimicrobial peptides
- POPG
- LL-37
- Self-assembly
- SAXS
- Cryo-TEM
- Coarse-grain molecular dynamics simulations
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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