Cyclodextrin‐Induced Suppression of PEG Crystallization from the Melt in a PEG‐Peptide Conjugate

The influence of alpha‐cyclodextrin (αCD) on PEG crystallization is examined for a peptide‐PEG conjugate, YYKLVFF‐PEG3k comprising an amyloid peptide YYKLVFF linked to PEG with molar mass 3 kg mol−1. Remarkably, differential scanning calorimetry (DSC) and simultaneous synchrotron small‐angle/wide‐an...

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Bibliographic Details
Published in:Chembiochem : a European journal of chemical biology 2024-10, Vol.25 (19), p.e202400396-n/a
Main Authors: Hamley, Ian W., Castelletto, Valeria, Hermida‐Merino, Daniel, Rosenthal, Martin
Format: Article
Language:English
Subjects:
Addition polymerization
Calorimetry
Conjugates
Crystallization
Cyclodextrin
Cyclodextrins
Differential scanning calorimetry
Hybrids
PEG
Peptide conjugate
Peptides
Polyethylene glycol
Polymers
Protein structure
SAXS/WAXS
β-Amyloid
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Summary:The influence of alpha‐cyclodextrin (αCD) on PEG crystallization is examined for a peptide‐PEG conjugate, YYKLVFF‐PEG3k comprising an amyloid peptide YYKLVFF linked to PEG with molar mass 3 kg mol−1. Remarkably, differential scanning calorimetry (DSC) and simultaneous synchrotron small‐angle/wide‐angle X‐ray scattering (SAXS/WAXS) show that crystallization of PEG is suppressed by αCD, provided that the cyclodextrin content is sufficient. A hexagonal mesophase is formed instead. The αCD threading reduces the conformational flexibility of PEG, and hence suppresses crystallization. These results show that addition of cyclodextrins can be used to tune the crystallization of peptide‐polymer conjugates and potentially other polymer/biomolecular hybrids. The influence of α‐cyclodextrin (αCD) on crystallization of PEG in an amyloid peptide‐PEG conjugate is investigated by SAXS/WAXS and DSC. The crystallization of PEG is suppressed (with sufficiently high αCD content in the blends) due to complexation with αCD, leading to hexagonal mesophase formation.
ISSN:1439-4227
1439-7633
1439-7633
DOI:10.1002/cbic.202400396