<i>De novo</i> designed peptides form a highly catalytic ordered nanoarchitecture on a graphite surface

Luo, Wei; Noguchi, Hironaga; Chen, Chen; Nakamura, Yoshiki; Homma, Chishu; Zozulia, Oleksii; Korendovych, Ivan V.; Hayamizu, Yuhei

doi:10.1039/d2nr01507b

Cited by 5 publications

(3 citation statements)

References 46 publications

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“…The AFM observations supported this expectation based on the height of the self-assembled structure of peptides. Taking advantage of these peptide conformations and stability, similar to previously reported works, − their ability to functionalize surfaces or act as probes can be regulated for further applications of biosensing and biotechnology.…”

Section: Resultssupporting

confidence: 60%

“…22 Recently, there have been few works on immobilizing these histidine-rich peptides on solid surfaces to construct bioelectrocatalysts as mimetic peroxidase enzymes. 23 These works demonstrate their ability to form hierarchical structures on the solid surface, which would open a new possibility in the applications of functionalized graphitic surfaces and establish potential nanoarchitectures for bioengineering and biotechnologies. However, the effect of peptide sequences on the selfassembly behavior has not been investigated.…”

Section: ■ Introductionmentioning

confidence: 91%

“…Scientists are trying to design histidine-rich peptides with amphiphilic properties that can be loaded by graphene to establish cell-penetrating engineering and drug nanocarriers . Recently, there have been few works on immobilizing these histidine-rich peptides on solid surfaces to construct bioelectrocatalysts as mimetic peroxidase enzymes . These works demonstrate their ability to form hierarchical structures on the solid surface, which would open a new possibility in the applications of functionalized graphitic surfaces and establish potential nanoarchitectures for bioengineering and biotechnologies.…”

Section: Introductionmentioning

confidence: 99%

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Rational Design and Self-Assembly of Histidine-Rich Peptides on a Graphite Surface

2023

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Histidine-rich peptides (HRPs) have been investigated to create functional biomolecules based on the nature of histidine, such as ion binding and catalytic activity. The organization of these HRPs on a solid surface can lead to surface functionalization with the well-known properties of HRPs. However, immobilization of HRPs on the surface has not been realized. Here, we design a series of octapeptides with histidine repeat units, aiming to establish their self-assembly on a graphite surface to produce a highly robust and active nanoscaffold. The new design has (XH)4, and we incorporated various types of hydrophobic amino acids at X in the sequence to facilitate their interaction with the surface. The effect of the pair of amino acids on their self-assembly was investigated by atomic force microscopy. Contact angle measurement revealed that these assemblies functionalized graphite surfaces with different wetting chemistry. Moreover, the secondary structure of peptides was characterized by Fourier transform infrared spectroscopy (FTIR), which gives us further insights into the conformation of histidine repeat peptides on the surface. Our results showed a new approach to applying histidine-rich peptides on the surface and tuning the self-assembly behavior by introducing different counter amino acids that could be integrated with a wide range of biosensing and biotechnology applications.

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Section: Resultssupporting

confidence: 60%

Section: ■ Introductionmentioning

confidence: 91%

Section: Introductionmentioning

confidence: 99%

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Rational Design and Self-Assembly of Histidine-Rich Peptides on a Graphite Surface

2023

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Peptides and metal ions: A successful marriage for developing artificial metalloproteins

Leone,

De Fenza,

Esposito

et al. 2024

Journal of Peptide Science

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The mutual relationship between peptides and metal ions enables metalloproteins to have crucial roles in biological systems, including structural, sensing, electron transport, and catalytic functions. The effort to reproduce or/and enhance these roles, or even to create unprecedented functions, is the focus of protein design, the first step toward the comprehension of the complex machinery of nature. Nowadays, protein design allows the building of sophisticated scaffolds, with novel functions and exceptional stability. Recent progress in metalloprotein design has led to the building of peptides/proteins capable of orchestrating the desired functions of different metal cofactors. The structural diversity of peptides allows proper selection of first‐ and second‐shell ligands, as well as long‐range electrostatic and hydrophobic interactions, which represent precious tools for tuning metal properties. The scope of this review is to discuss the construction of metal sites in de novo designed and miniaturized scaffolds. Selected examples of mono‐, di‐, and multi‐nuclear binding sites, from the last 20 years will be described in an effort to highlight key artificial models of catalytic or electron‐transfer metalloproteins. The authors' goal is to make readers feel like guests at the marriage between peptides and metal ions while offering sources of inspiration for future architects of innovative, artificial metalloproteins.

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Simulating chemical reactions promoted by self-assembled peptides with catalytic properties

Yang,

Wang,

Dong

2024

Methods in Enzymology

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De novo designed peptides form a highly catalytic ordered nanoarchitecture on a graphite surface

Abstract: Here we demonstrate that short peptides, de novo designed from the first principles, self-assemble on the surface of graphite to produce highly robust and catalytic nanoarchitechture, which promotes peroxidation reactions...

Cited by 5 publications

References 46 publications

Rational Design and Self-Assembly of Histidine-Rich Peptides on a Graphite Surface

Rational Design and Self-Assembly of Histidine-Rich Peptides on a Graphite Surface

Peptides and metal ions: A successful marriage for developing artificial metalloproteins

Simulating chemical reactions promoted by self-assembled peptides with catalytic properties

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