Cyclodextrin-Based Polymeric Materials Bound to Corona Protein for Theranostic Applications

Abstract

Cyclodextrins (CDs) are cyclic oligosaccharide structures that could be used for theranostic applications in personalized medicine. These compounds have been widely utilized not only for enhancing drug solubility, stability, and bioavailability but also for controlled and targeted delivery of small molecules. These compounds can be complexed with various biomolecules, such as peptides or proteins, via host-guest interactions. CDs are amphiphilic compounds with water-hating holes and water-absorbing surfaces. Architectures of CDs allow the drawing and preparation of CD-based polymers (CDbPs) with optimal pharmacokinetic and pharmacodynamic properties. These polymers can be cloaked with protein corona consisting of adsorbed plasma or extracellular proteins to improve nanoparticle biodistribution and half-life. Besides, CDs have become famous in applications ranging from biomedicine to environmental sciences. In this review, we emphasize ongoing research in biomedical fields using CD-based centered, pendant, and terminated polymers and their interactions with protein corona for theranostic applications. Overall, a perusal of information concerning this novel approach in biomedicine will help to implement this methodology based on host-guest interaction to improve therapeutic and diagnostic strategies.

Keywords: cyclodextrin; nanomedicine; polymers; protein corona; theranostics; therapy.

Figure 1

Structure and conformation of natural CDs.

Figure 2

Diagram describes the production process of drug-loaded single-chain polymer nanoparticles (SCNPs) for dual-responsive drug release [38]. The abbreviations are PDI*: perylenediimide, PCL: polycaprolactone, PEG: polyethyleneglycol, and GSH: glutathione.

Figure 3

The interaction between protein corona, NP, and cellular receptors (physiological reactions). After NP injection into the blood, protein corona starts to aggregate at the NP surface as a part of biological identity. After that, cellular response can be triggered by specific protein receptors at the cell surface [44,45].

Figure 4

Classification of polymers by molecular topology.

Figure 5

The kinetic proceeding of protein amyloid fibrillation comprising (Lag phase) aggregation of misfolded monomers into tiny intermediate oligomers; (Growth phase) re-arrangement of these oligomers into organized fibrils containing the cross-beta structure; (Saturation phase) association of beta structured oligomers into proto-fibrils [120].