Cysteine Redox Chemistry in Peptide Self-Assembly to Modulate Hydrogelation

Cringoli, Maria Cristina; Marchesan, Silvia

doi:10.3390/molecules28134970

Cited by 7 publications

(3 citation statements)

References 109 publications

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“…Inspired by the self-assembly of proteins and peptides, − amino acids, as the basic units of these biomolecules, can self-assemble through noncovalent interactions and form various structures with attractive physical and chemical properties, as well as diverse morphologies, including nanotubes, nanoribbons, nanofibers, nanovesicles, etc. In this review, we have summarized the rational design as well as recent advances of amino acid based materials for bionanotechnology applications.…”

Section: Conclusion and Perspectivesmentioning

confidence: 99%

Bioinspired Amino Acid Based Materials in Bionanotechnology: From Minimalistic Building Blocks and Assembly Mechanism to Applications

Wang,

Rencus-Lazar,

Zhou

et al. 2023

ACS Nano

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Inspired by natural hierarchical self-assembly of proteins and peptides, amino acids, as the basic building units, have been shown to self-assemble to form highly ordered structures through supramolecular interactions. The fabrication of functional biomaterials comprised of extremely simple biomolecules has gained increasing interest due to the advantages of biocompatibility, easy functionalization, and structural modularity. In particular, amino acid based assemblies have shown attractive physical characteristics for various bionanotechnology applications. Herein, we propose a review paper to summarize the design strategies as well as research advances of amino acid based supramolecular assemblies as smart functional materials. We first briefly introduce bioinspired reductionist design strategies and assembly mechanism for amino acid based molecular assembly materials through noncovalent interactions in condensed states, including self-assembly, metal ion mediated coordination assembly, and coassembly. In the following part, we provide an overview of the properties and functions of amino acid based materials toward applications in nanotechnology and biomedicine. Finally, we give an overview of the remaining challenges and future perspectives on the fabrication of amino acid based supramolecular biomaterials with desired properties. We believe that this review will promote the prosperous development of innovative bioinspired functional materials formed by minimalistic building blocks.

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Section: Conclusion and Perspectivesmentioning

confidence: 99%

Bioinspired Amino Acid Based Materials in Bionanotechnology: From Minimalistic Building Blocks and Assembly Mechanism to Applications

Wang,

Rencus-Lazar,

Zhou

et al. 2023

ACS Nano

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“…The sulfhydryl group of cysteine is unique among all amino acids and plays a crucial role in the structure and function of proteins and peptides . Researchers investigate how sulfhydryl groups affect peptide self-assembly as well as how redox regulation controls changes in solution and gel . To cause gelation, disulfide cross-links have been used in numerous investigations.…”

Section: Introductionmentioning

confidence: 99%

“…7 Researchers investigate how sulfhydryl groups affect peptide self-assembly as well as how redox regulation controls changes in solution and gel. 8 To cause gelation, disulfide cross-links have been used in numerous investigations. According to Dong et al, sulfhydryl-rich peptides create internal disulfide bonds upon oxidation, and the development of β-turn structure encourages the peptide to self-assemble into a mechanically rigid hydrogel that is transformed into a solution when the disulfide bonds are opened by reduction.…”

Section: ■ Introductionmentioning

confidence: 99%

Gel-to-Solution Transition of Sulfhydryl Self-Assembled Peptide Hydrogels Undergoing Oxidative Modulation

Hu,

Liu,

Shen

2023

ACS Appl. Bio Mater.

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Metal Ions Trigger the Gelation of Cysteine‐Containing Peptide‐Appended Coordination Cages

Li,

Zhu,

Adorinni

et al. 2024

Angewandte Chemie

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We report a series of coordination cages that incorporate peptide chains at their vertices, prepared through subcomponent self‐assembly. Three distinct heterochiral tripeptide subcomponents were incorporated, each exhibiting an L–D–L stereoconfiguration. Through this approach, we prepared and characterized three tetrahedral metal‐peptide cages that incorporate thiol and methylthio groups. The gelation of these cages wasprobed through the binding of additional metal ions, with the metal‐peptide cages acting as junctions, owing to the presence of sulfur atoms on the peripheral peptides. Gels were obtained with cages bearing cysteine at the C‐terminus. Our strategy for developing functional metal‐coordinated supramolecular gels with a modular design may result in the development of materials useful for chemical separations or drug delivery.

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Cysteine Redox Chemistry in Peptide Self-Assembly to Modulate Hydrogelation

Cited by 7 publications

References 109 publications

Bioinspired Amino Acid Based Materials in Bionanotechnology: From Minimalistic Building Blocks and Assembly Mechanism to Applications

Bioinspired Amino Acid Based Materials in Bionanotechnology: From Minimalistic Building Blocks and Assembly Mechanism to Applications

Gel-to-Solution Transition of Sulfhydryl Self-Assembled Peptide Hydrogels Undergoing Oxidative Modulation

Metal Ions Trigger the Gelation of Cysteine‐Containing Peptide‐Appended Coordination Cages

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