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Thio‐Bromo “Click” Reaction Derived Polymer–Peptide Conjugates for Their Self‐Assembled Fibrillar Nanostructures
Author(s) -
Kumar Sonu,
Hause Gerd,
Binder Wolfgang H.
Publication year - 2020
Publication title -
macromolecular bioscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.924
H-Index - 105
eISSN - 1616-5195
pISSN - 1616-5187
DOI - 10.1002/mabi.202000048
Subject(s) - chemistry , peptide , click chemistry , ethylene glycol , circular dichroism , amphiphile , electrospray ionization , self assembly , polymer , conjugate , combinatorial chemistry , supramolecular chemistry , mass spectrometry , polymer chemistry , copolymer , organic chemistry , chromatography , stereochemistry , mathematical analysis , biochemistry , crystal structure , mathematics
The synthesis and self‐assembly of peptide–polymer conjugates into fibrillar nanostructures are reported, based on the amyloidogenic peptide KLVFF. A strategy for rational synthesis of polymer–peptide conjugates is documented via tethering of the amyloidogenic peptide segment LVFF (Aβ 17‐20 ) and its modified derivative FFFF to the hydrophilic poly(ethylene glycol) monomethyl ether (mPEG) polymer via thio‐bromo based “click” chemistry. The resultant conjugates mPEG‐LVFF‐OMe and mPEG‐FFFF‐OMe are purified via preparative gel permeation chromatography technique (with a yield of 61% and 64%, respectively), and are successfully characterized via combination of spectroscopic and chromatographic methods, including electrospray ionization time‐of‐flight mass spectrometry. The peptide‐guided self‐assembling behavior of the as‐constructed amphiphilic supramolecular materials is further investigated via transmission electron microscopic and circular dichroism spectroscopic analysis, exhibiting fibrillar nanostructure formation in binary aqueous solution mixture.