FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2401183379> ?p ?o ?g. }

• W2401183379 abstract "Peptide-membrane interactions play an important role in many biological systems, drug delivery systems and therapeutics. Examples include antimicrobial peptides, which show promise as alternatives to conventional antibiotics, and cell-penetrating peptides, which can pass though the plasma membrane of cells and therefore have the potential for use in drug delivery. However, the precise mechanisms of these interactions is still uncertain and, in particular, there is limited understanding of the role that the membrane and its structure plays in these interactions. Dual-polarization interferometry (DPI) is a recently developed optical technique that can simultaneously measure multiple properties of a layer adsorbed to the surface of a chip. Here, the mass and birefringence (a measure of bilayer structure) of a supported lipid bilayer are measured simultaneously in real time during the binding and subsequent dissociation of certain peptides. A novel analysis technique is then used to fit a kinetic model simultaneously to the mass and birefringence data thus obtained. Depending on the data observed, the most appropriate model may be either two-state or three-state (in terms of distinct bound peptide states) with or without adjustments to account for lateral bilayer expansion, lag in birefringence changes from peptide binding, and mass thresholds for state transitions. These methods are used to investigate the membrane binding of several model peptides. For the binding mechanism of the antimicrobial peptide HPA3 it is found that a two-state model is sufficient for its binding to gel-phase membranes, while a three-state model with bilayer expansion is necessary for fluid-phase membranes. The binding of the magainin 2 analogue varied depending on the membrane type, but where a suitably accurate fit was obtained, a three-state model with bilayer expansion was needed, with birefringence lag in some cases. The cell-penetrating peptide penetratin and a truncated analogue R8K-biotin were compared, with R8K-biotin fitted by a two-state model while penetratin required a three-state model, which is indicative of a more complex and involved binding process. The binding of helix 8 of the angiotensin receptor was compared for membranes with or without phosphatidylinositol phosphates (PIPs); there was a dramatic change in the binding between membranes with and without PIPs, indicating a significant interaction between Helix 8 and PIPs. For each of these peptide types, a hypothesis about the binding mechanism is formed from the data obtained through modelling. Additionally, testing is performed to measure the level of variability of the modelling, both as a result of intrinsic uncertainties in the modelling itself, and variations in the data obtained between different experimental runs. This new modelling technique allows for powerful quantitative characterisation of DPI data, and provides new insights into peptide-membrane interactions that are likely to improve scientific understanding of these systems and assist the development of therapeutic products associated with them." @default.
• W2401183379 created "2016-06-24" @default.
• W2401183379 creator A5084793666 @default.
• W2401183379 date "2017-02-27" @default.
• W2401183379 modified "2023-09-27" @default.
• W2401183379 title "Kinetic modelling techniques for simultaneous mass and structural changes during peptide-membrane interactions" @default.
• W2401183379 doi "https://doi.org/10.4225/03/58b36fa2b7ec2" @default.
• W2401183379 hasPublicationYear "2017" @default.
• W2401183379 type Work @default.
• W2401183379 sameAs 2401183379 @default.
• W2401183379 citedByCount "0" @default.
• W2401183379 crossrefType "dissertation" @default.
• W2401183379 hasAuthorship W2401183379A5084793666 @default.
• W2401183379 hasConcept C120665830 @default.
• W2401183379 hasConcept C121332964 @default.
• W2401183379 hasConcept C12554922 @default.
• W2401183379 hasConcept C125743686 @default.
• W2401183379 hasConcept C159467904 @default.
• W2401183379 hasConcept C185592680 @default.
• W2401183379 hasConcept C192157962 @default.
• W2401183379 hasConcept C2779281246 @default.
• W2401183379 hasConcept C39944091 @default.
• W2401183379 hasConcept C41625074 @default.
• W2401183379 hasConcept C540938839 @default.
• W2401183379 hasConcept C55493867 @default.
• W2401183379 hasConcept C86803240 @default.
• W2401183379 hasConceptScore W2401183379C120665830 @default.
• W2401183379 hasConceptScore W2401183379C121332964 @default.
• W2401183379 hasConceptScore W2401183379C12554922 @default.
• W2401183379 hasConceptScore W2401183379C125743686 @default.
• W2401183379 hasConceptScore W2401183379C159467904 @default.
• W2401183379 hasConceptScore W2401183379C185592680 @default.
• W2401183379 hasConceptScore W2401183379C192157962 @default.
• W2401183379 hasConceptScore W2401183379C2779281246 @default.
• W2401183379 hasConceptScore W2401183379C39944091 @default.
• W2401183379 hasConceptScore W2401183379C41625074 @default.
• W2401183379 hasConceptScore W2401183379C540938839 @default.
• W2401183379 hasConceptScore W2401183379C55493867 @default.
• W2401183379 hasConceptScore W2401183379C86803240 @default.
• W2401183379 hasLocation W24011833791 @default.
• W2401183379 hasOpenAccess W2401183379 @default.
• W2401183379 hasPrimaryLocation W24011833791 @default.
• W2401183379 hasRelatedWork W1483517598 @default.
• W2401183379 hasRelatedWork W1585661352 @default.
• W2401183379 hasRelatedWork W1968299564 @default.
• W2401183379 hasRelatedWork W1977864203 @default.
• W2401183379 hasRelatedWork W2003202907 @default.
• W2401183379 hasRelatedWork W2015659341 @default.
• W2401183379 hasRelatedWork W2019317580 @default.
• W2401183379 hasRelatedWork W2021966802 @default.
• W2401183379 hasRelatedWork W2063610611 @default.
• W2401183379 hasRelatedWork W2068659658 @default.
• W2401183379 hasRelatedWork W2081669939 @default.
• W2401183379 hasRelatedWork W2085398302 @default.
• W2401183379 hasRelatedWork W2103752673 @default.
• W2401183379 hasRelatedWork W2156144788 @default.
• W2401183379 hasRelatedWork W2583795543 @default.
• W2401183379 hasRelatedWork W2583838678 @default.
• W2401183379 hasRelatedWork W2807137729 @default.
• W2401183379 hasRelatedWork W2956174187 @default.
• W2401183379 hasRelatedWork W3049356164 @default.
• W2401183379 hasRelatedWork W2184681623 @default.
• W2401183379 isParatext "false" @default.
• W2401183379 isRetracted "false" @default.
• W2401183379 magId "2401183379" @default.
• W2401183379 workType "dissertation" @default.