Modulation of phase transition of thermosensitive liposomes with leucine zipper-structured lipopeptides

Targeted therapy for cancer requires thermosensitive components in drug carriers for controlled drug release against viral cells. The conformational transition characteristic of leucine zipper-structured lipopeptides is utilized in our lab to modulate the phase transition temperature of liposomes, t...

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Bibliographic Details
Published in:Physical chemistry chemical physics : PCCP 2018, Vol.20 (23), p.15916-15925
Main Authors: Xu, Xiejun, Xiao, Xingqing, Wang, Yiming, Xu, Shouhong, Liu, Honglai
Format: Article
Language:English
Subjects:
Binding
Computer simulation
Dihedral angle
Dimers
Drug carriers
Drug delivery systems
Dynamic stability
Dynamic structural analysis
Functional groups
Hydrogen bonds
Leucine
Liposomes
Molecular chains
Molecular dynamics
Phase transitions
Principal components analysis
Proteins
Structural analysis
Temperature
Trajectory analysis
Transition temperature
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Summary:Targeted therapy for cancer requires thermosensitive components in drug carriers for controlled drug release against viral cells. The conformational transition characteristic of leucine zipper-structured lipopeptides is utilized in our lab to modulate the phase transition temperature of liposomes, thus achieving temperature-responsive control. In this study, we computationally examined the conformational transition behaviors of leucine zipper-structured lipopeptides that were modified at the N-terminus by distinct functional groups. The conformational transition temperatures of these lipopeptides were determined by structural analysis of the implicit-solvent replica exchange molecular dynamics simulation trajectories using the dihedral angle principal component analysis and the dictionary of protein secondary structure method. Our calculations revealed that the computed transition temperatures of the lipopeptides are in good agreement with the experimental measurements. The effect of hydrogen bonds on the conformational stability of the lipopeptide dimers was examined in conventional explicit-solvent molecular dynamics simulations. A quantitative correlation of the degree of structural dissociation of the dimers and their binding strength is well described by an exponential fit of the binding free energies to the conformation transition temperatures of the lipopeptides.
ISSN:1463-9076
1463-9084
DOI:10.1039/c8cp01464g