Affordable Access

Access to the full text

Antimicrobial peptide induced colloidal transformations in bacteria-mimetic vesicles : combining in silico tools and experimental methods

Authors
  • Freire, Rafael V.M.
  • Pillco-Valencia, Yeny
  • da Hora, Gabriel C.A.
  • Ramstedt, Madeleine
  • Sandblad, Linda
  • Soares, Thereza A.
  • Salentinig, Stefan
Publication Date
Jan 01, 2021
Identifiers
DOI: 10.1016/j.jcis.2021.03.060
OAI: oai:DiVA.org:umu-182119
Source
DiVA - Academic Archive On-line
Keywords
Language
English
License
Green
External links

Abstract

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.

Report this publication

Statistics

Seen <100 times