Rational Design and Self-Assembly of Histidine-Rich Peptides on a Graphite Surface-Reference-Cited by-同舟云学术

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

Published:2023-05-12 Issue:20 Volume:39 Page:7057-7062
ISSN:0743-7463
Container-title:Langmuir
language:en
Short-container-title:Langmuir

Author:

Luo Wei¹,Homma Chishu¹,Hayamizu Yuhei¹^ORCID

Affiliation:

1. Department of Materials Science and Engineering, School of Materials and Chemical Technology, Tokyo Institute of Technology, 2-12-1 Ookayama, Meguroku, Tokyo 152-8550, Japan

Funder

Precise Measurement Technology Promotion Foundation

Japan Society for the Promotion of Science

China Scholarship Council

Publisher

American Chemical Society (ACS)

Subject

Electrochemistry,Spectroscopy,Surfaces and Interfaces,Condensed Matter Physics,General Materials Science

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.langmuir.3c00270

Reference39 articles.

1. Interactions of histidine and other imidazole derivatives with transition metal ions in chemical and biological systems

2. Exploring mussel byssus fabrication with peptide-polymer hybrids: Role of pH and metal coordination in self-assembly and mechanics of histidine-rich domains

3. Short peptides self-assemble to produce catalytic amyloids

4. The amyloid architecture provides a scaffold for enzyme-like catalysts

5. Humanserumproteine mit hoher Affinität zu Carboxymethylcellulose, II. Physikalisch-chemische und immunologische Charakterisierung eines histidinreichen 3,8S-α2-Glykoproteins (CM-Protein I)

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