Harnessing supramolecular peptide nanotechnology in biomedical applications

Chan, Kiat Hwa; Lee, Wei Hao; Zhuo, Shuangmu; Ni, Ming

doi:10.2147/ijn.s126154

Cited by 41 publications

(27 citation statements)

References 122 publications

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“…Nonetheless, the structural information we have uncovered for Ac-LLE and Ac-YLD, as well as the self-assembly outcomes due to the single moiety changes to various tripeptides, can potentially be used to provide vital data to design and assemble novel peptide nanostructures. These novel peptide nanostructures can then be assessed under physiological conditions for their applicability in diverse biomedical applications 89 .…”

Section: Discussionmentioning

confidence: 99%

Systematic Moiety Variations of Ultrashort Peptides Produce Profound Effects on Self-Assembly, Nanostructure Formation, Hydrogelation, and Phase Transition

Chan

Xue

Robinson

et al. 2017

Sci Rep

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Self-assembly of small biomolecules is a prevalent phenomenon that is increasingly being recognised to hold the key to building complex structures from simple monomeric units. Small peptides, in particular ultrashort peptides containing up to seven amino acids, for which our laboratory has found many biomedical applications, exhibit immense potential in this regard. For next-generation applications, more intricate control is required over the self-assembly processes. We seek to find out how subtle moiety variation of peptides can affect self-assembly and nanostructure formation. To this end, we have selected a library of 54 tripeptides, derived from systematic moiety variations from seven tripeptides. Our study reveals that subtle structural changes in the tripeptides can exert profound effects on self-assembly, nanostructure formation, hydrogelation, and even phase transition of peptide nanostructures. By comparing the X-ray crystal structures of two tripeptides, acetylated leucine-leucine-glutamic acid (Ac-LLE) and acetylated tyrosine-leucine-aspartic acid (Ac-YLD), we obtained valuable insights into the structural factors that can influence the formation of supramolecular peptide structures. We believe that our results have major implications on the understanding of the factors that affect peptide self-assembly. In addition, our findings can potentially assist current computational efforts to predict and design self-assembling peptide systems for diverse biomedical applications.

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Section: Discussionmentioning

confidence: 99%

Systematic Moiety Variations of Ultrashort Peptides Produce Profound Effects on Self-Assembly, Nanostructure Formation, Hydrogelation, and Phase Transition

Chan

Xue

Robinson

et al. 2017

Sci Rep

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“…However, the main challenge that might hinder the translation to clinical settings remains the antigenicity of the utilized cells and biomaterials that might trigger the body's immunogenic response. 54 These obstacles have been overcome in the present study, as the biocompatibility of the construct has been proved in vitro as well as in vivo. Further studies will be required to provide the intra-articular functional evidence of the construct.…”

Section: Dovepressmentioning

confidence: 94%

<p>Nanoscale Thermosensitive Hydrogel Scaffolds Promote the Chondrogenic Differentiation of Dental Pulp Stem and Progenitor Cells: A Minimally Invasive Approach for Cartilage Regeneration</p>

Talaat¹,

Ac²,

Kawas³

et al. 2020

IJN

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Purpose: Several scaffolds and cell sources are being investigated for cartilage regeneration. The aim of the study was to prepare nanocellulose-based thermosensitive injectable hydrogel scaffolds and assess their potential as 3D scaffolds allowing the chondrogenic differentiation of embedded human dental pulp stem and progenitor cells (hDPSCs). Materials and Methods: The hydrogel-forming solutions were prepared by adding βglycerophosphate (GP) to chitosan (CS) at different ratios. Nanocellulose (NC) suspension was produced from hemp hurd then added dropwise to the CS/GP mixture. In vitro characterization of the prepared hydrogels involved optimizing gelation and degradation time, massswelling ratio, and rheological properties. The hydrogel with optimal characteristics, NC-CS /GP-21, was selected for further investigation including assessment of biocompatibility. The chondrogenesis ability of hDPSCs embedded in NC-CS/GP-21 hydrogel was investigated in vitro and compared to that of bone marrow-derived mesenchymal stem cells (BMSCs), then was confirmed in vivo in 12 adult Sprague Dawley rats. Results: The selected hydrogel showed stability in culture media, had a gelation time of 2.8 minutes, showed a highly porous microstructure by scanning electron microscope, and was morphologically intact in vivo for 14 days after injection. Histological and immunohistochemical analyses and real-time PCR confirmed the chondrogenesis ability of hDPSCs embedded in NC-CS/GP-21 hydrogel. Conclusion: Our results suggest that nanocellulose-chitosan thermosensitive hydrogel is a biocompatible, injectable, mechanically stable and slowly degradable scaffold. hDPSCs embedded in NC-CS/GP-21 hydrogel is a promising, minimally invasive, stem cell-based strategy for cartilage regeneration.

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“…Various higher order structures have been observed before, including nanotapes, nanotubes, nanoparticles, and nanofibrils 18 – 21 . Among these nanostructures, nanofibrils play a prominent role in many biomedical applications 22 – 24 .…”

Section: Introductionmentioning

confidence: 90%

C-Terminal Residue of Ultrashort Peptides Impacts on Molecular Self-Assembly, Hydrogelation, and Interaction with Small-Molecule Drugs

Chan

Lee

et al. 2018

Sci Rep

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Single molecular changes on a tripeptide can have dramatic effects on their self-assembly and hydrogelation. Herein, we explore C-terminal residue variation on two consistent ultrashort peptide backbones, i.e. acetylated-Leu-Ile-Val-Ala-Gly-Xaa and acetylated-Ile-Val-Xaa (Xaa = His, Arg, Asn). The objective of this study is to identify candidates that can form hydrogels for small-molecule drug (SMD) delivery. Haemolysis and cytotoxicity (with human adipose-derived mesenchymal stem cells) assays showed that the new soluble peptides (Xaa = His, Arg) are cytocompatible. Gelation studies showed that all but acetylated-Ile-Val-Arg could gel under physiological conditions. Longer peptidic backbones drive self-assembly more effectively as reflected in field emission scanning electron microscopy (FESEM) and circular dichroism spectroscopy studies. Rheological studies revealed that the resultant hydrogels have varying stiffness and yield stress, depending on the backbone and C-terminal residue. Visible spectroscopy-based elution studies with SMDs (naltrexone, methotrexate, doxorubicin) showed that besides the C-terminal residue, the shape of the SMD also determines the rate and extent of SMD elution. Based on the elution assays, infrared spectroscopy, and FESEM, we propose models for the peptide fibril-SMD interaction. Our findings highlight the importance of matching the molecular properties of the self-assembling peptide and SMD in order to achieve the desired SMD release profile.

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Harnessing supramolecular peptide nanotechnology in biomedical applications

Cited by 41 publications

References 122 publications

Systematic Moiety Variations of Ultrashort Peptides Produce Profound Effects on Self-Assembly, Nanostructure Formation, Hydrogelation, and Phase Transition

Systematic Moiety Variations of Ultrashort Peptides Produce Profound Effects on Self-Assembly, Nanostructure Formation, Hydrogelation, and Phase Transition

<p>Nanoscale Thermosensitive Hydrogel Scaffolds Promote the Chondrogenic Differentiation of Dental Pulp Stem and Progenitor Cells: A Minimally Invasive Approach for Cartilage Regeneration</p>

C-Terminal Residue of Ultrashort Peptides Impacts on Molecular Self-Assembly, Hydrogelation, and Interaction with Small-Molecule Drugs

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