Aggregation Induced α-Helix/β-Sheet Transition of the Poly(ethylene glycol)-attached Peptide

Tanaka, Masayoshi; Abiko, Souhei; Koga, Tomoyuki; Koshikawa, Naokiyo; Kinoshita, Takatoshi

doi:10.1295/polymj.pj2008179

Cited by 1 publication

(1 citation statement)

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“…Since the early 1950s, when Jatzkewitz described the first example of a peptide/polymer conjugate, several reviews, communications, and perspectives on their synthesis and potential applications have been reported. It has been observed that the conjugation of polymers (with particular reference to PEG chains) to natural or synthetic peptides such as poly(γ‐benzyl‐ l ‐aspartate), [(AG) 3 EG] 10 , DGRFFF, (LELL) 4 , and oligo(phenylalanines) can strongly affect their structural properties. Moreover, owing to the crystallization phenomenon, PEG could inhibit the fibrillation of amyloid peptide sequences (i.e., Aβ 16‐20 and Aβ 10‐35 ), a function not available to the unmodified peptide.…”

Section: Introductionmentioning

confidence: 99%

Structural Characterization of PEGylated Hexaphenylalanine Nanostructures Exhibiting Green Photoluminescence Emission

Diaferia

Sibillano

Altamura

et al. 2017

Chemistry A European J

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Peptides containing aromatic residues are known to exhibit spontaneous phenomena of supramolecular organization into ordered nanostructures (NSs). In this work we studied the structural behavior and optoelectronic properties of new biocompatible materials obtained by the self-assembly of a series of hexaphenylalanines (F6) modified at the N terminus by a PEG chain of different lengths. PEG -F6, PEG -F6, and PEG -F6 peptides were synthesized by coupling sequentially two, three, or four units of amino-carboxy-PEG blocks, each one containing six oxyethylene repetitions. Changes in the length and composition of the PEG chain were found to modulate the structural organization of the phenylalanine-based nanostructures. An increase in the self-aggregation tendency was observed with longer PEG chains, whereas, independently of the PEG length, the peptide NSs display cross-β-like secondary structures with an antiparallel β-strand arrangement. WAXS/GIWAXS diffraction patterns indicate a progressive decrease in fiber order along the series. All the PEG-F6 derivatives present blue photoluminescent (PL) emission at 460 nm, with the adduct with the longest PEG chain (PEG -F6) showing an additional green emission at 530 nm.

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