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Directed Assembly of Elastin-like Proteins into defined Supramolecular Structures and Cargo Encapsulation In Vitro
Published on: April 8, 2020
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Refining the Design of Diblock Elastin-Like Polypeptides for Self-Assembly into Nanoparticles
Michèle Dai1,2, Evangelos Georgilis1,3, Guillaume Goudounet1
1University Bordeaux, CNRS, Bordeaux INP, LCPO, UMR 5629, 33600 Pessac, France.
Polymers
|June 2, 2021
Summary
Researchers designed elastin-like polypeptide (ELP) diblock copolymers for drug delivery. Selective oxidation of ELP-[M1V3-i]-[I-j] diblocks enabled controlled thermal phase transitions, forming unimers, micelles, and aggregates for cargo delivery.
Area of Science:
- Biomaterials Science
- Polymer Chemistry
- Drug Delivery Systems
Background:
- Elastin-like polypeptides (ELPs) are stimuli-responsive biopolymers.
- ELPs exhibit tunable phase transitions upon thermal stimulation.
- ELP-based carriers offer potential for targeted active molecule delivery.
Purpose of the Study:
- To design and investigate a library of ELP diblock copolymers.
- To explore the self-assembly and phase transition behavior of novel ELP diblocks.
- To establish controlled formation of unimers, micelles, and aggregates for cargo encapsulation.
Main Methods:
- Synthesis of ELP diblock copolymers with varying sequences (ELP-[M1V3-i]-[I-j]).
- Selective oxidation of methionine residues within the ELP diblock structures.
- Characterization of self-assembly and thermal phase transition properties.
Main Results:
- ELP-[M1V3-i]-[I-j] diblocks demonstrated similar self-assembly to monoblocks.
- Selective methionine oxidation unlocked distinct thermal phase transition regimes.
- Three regimes were observed: unimers, micelles, and aggregates, characteristic of well-defined ELP diblocks.
Conclusions:
- Designed ELP diblock copolymers exhibit controlled thermal phase transitions.
- Selective oxidation is a viable strategy to tune ELP diblock behavior.
- These findings pave the way for advanced ELP-based drug delivery systems.
Keywords:
elastin-like polypeptidesmethionine oxidationnanoparticlesself-assemblythermoresponsiveness
