Versatile design of amphiphilic glycopolypeptides nanoparticles for lectin recognition. (19th December 2016)
- Record Type:
- Journal Article
- Title:
- Versatile design of amphiphilic glycopolypeptides nanoparticles for lectin recognition. (19th December 2016)
- Main Title:
- Versatile design of amphiphilic glycopolypeptides nanoparticles for lectin recognition
- Authors:
- Gauche, Cony
Lecommandoux, Sébastien - Abstract:
- Abstract: The understanding of glycopolymer-based nanostructures formation and their lectin binding properties are of great interest to the development of drug delivery systems and other biological applications. Herein, glycosylated polypeptides were synthesized from a clickable poly(l -lysine)- b -poly(benzyl-l -glutamate) copolypeptide, obtained by a sequential ring opening polymerization. The clickable poly(l -lysine) chain was completely functionalized by introducing galactose and lactose moieties on the copolypeptide's hydrophilic block, aiming specific lectin recognition. Spheres, pearl-necklace and worm-like structures prepared from poly(l -lysine)- b -poly(benzyl-l -glutamate) copolypeptides were obtained after nanoprecipitation, depending on the hydrophilic block functionalization and the hydrophobic block length. Specific interaction between the sugars on the micelles' surface with RCA120 lectin was observed with the PBLG40-based nano-structures. However, unexpected and unspecific interactions were observed with some nanostructures, showing the importance of the chemical functionalization and nanostructure stabilization. Such a synthetic approach can be used to develop any other amphiphilic and biofunctional polypeptide-based copolymers and nanoparticles. Graphical abstract: Highlights: ROP and CuAAC reactions afforded fully functionalized PLys- b -PBLG-based glycocopolypeptides. Nanoparticles with different morphologies were obtained depending on block copolymerAbstract: The understanding of glycopolymer-based nanostructures formation and their lectin binding properties are of great interest to the development of drug delivery systems and other biological applications. Herein, glycosylated polypeptides were synthesized from a clickable poly(l -lysine)- b -poly(benzyl-l -glutamate) copolypeptide, obtained by a sequential ring opening polymerization. The clickable poly(l -lysine) chain was completely functionalized by introducing galactose and lactose moieties on the copolypeptide's hydrophilic block, aiming specific lectin recognition. Spheres, pearl-necklace and worm-like structures prepared from poly(l -lysine)- b -poly(benzyl-l -glutamate) copolypeptides were obtained after nanoprecipitation, depending on the hydrophilic block functionalization and the hydrophobic block length. Specific interaction between the sugars on the micelles' surface with RCA120 lectin was observed with the PBLG40-based nano-structures. However, unexpected and unspecific interactions were observed with some nanostructures, showing the importance of the chemical functionalization and nanostructure stabilization. Such a synthetic approach can be used to develop any other amphiphilic and biofunctional polypeptide-based copolymers and nanoparticles. Graphical abstract: Highlights: ROP and CuAAC reactions afforded fully functionalized PLys- b -PBLG-based glycocopolypeptides. Nanoparticles with different morphologies were obtained depending on block copolymer composition. Specific interaction between nanoparticles with lectins were observed. … (more)
- Is Part Of:
- Polymer. Volume 107(2016)
- Journal:
- Polymer
- Issue:
- Volume 107(2016)
- Issue Display:
- Volume 107, Issue 2016 (2016)
- Year:
- 2016
- Volume:
- 107
- Issue:
- 2016
- Issue Sort Value:
- 2016-0107-2016-0000
- Page Start:
- 474
- Page End:
- 484
- Publication Date:
- 2016-12-19
- Subjects:
- Copolymer -- Self-assembly -- Micelles
Polymers -- Periodicals
Polymerization -- Periodicals
Polymères -- Périodiques
Polymérisation -- Périodiques
547.7 - Journal URLs:
- http://www.sciencedirect.com/science/journal/00323861 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.polymer.2016.08.077 ↗
- Languages:
- English
- ISSNs:
- 0032-3861
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6547.700000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 2588.xml