Non-reducible disulfide bond replacement implies that disulfide exchange is not required for hepcidin–ferroportin interaction-Reference-Cited by-同舟云学术

Non-reducible disulfide bond replacement implies that disulfide exchange is not required for hepcidin–ferroportin interaction

Published:2019 Issue:19 Volume:55 Page:2821-2824
ISSN:1359-7345
Container-title:Chemical Communications
language:en
Short-container-title:Chem. Commun.

Author:

Huang Dong-Liang¹²³⁴⁵,Bai Jing-Si⁶⁷⁸⁹,Wu Meng¹²³⁴⁵,Wang Xia⁶⁷⁸⁹,Riedl Bernd¹⁰¹¹¹²¹³,Pook Elisabeth¹⁰¹⁴¹³,Alt Carsten¹⁰¹⁵¹³,Erny Marion¹⁰¹⁵¹³,Li Yi-Ming⁶⁷⁸⁹,Bierer Donald¹⁰¹¹¹²¹³,Shi Jing¹⁶¹⁷¹⁸⁹,Fang Ge-Min¹²³⁴⁵^ORCID

Affiliation:

1. School of Life Science

2. Institute of Health Science and Technology

3. Institutes of Physical Science and Information Technology

4. Anhui University

5. Hefei 230601

6. School of Food and Biological Engineering

7. Hefei University of Technology

8. Hefei 230009

9. P. R. China

10. Bayer AG

11. Department of Medicinal Chemistry

12. 42096 Wuppertal

13. Germany

14. Lead Discovery Wuppertal

15. Hematology Research

16. Department of Chemistry

17. University of Science and Technology of China

18. Hefei 230026

Abstract

Non-reducible disulfide bond replacement was used to study the disculfide exchange between hepcidin and ferroportin, and the results indicate that the hepcidin–ferroportin interaction does not require disfulfide exchange.

Funder

National Natural Science Foundation of China

Publisher

Royal Society of Chemistry (RSC)

Subject

Materials Chemistry,Metals and Alloys,Surfaces, Coatings and Films,General Chemistry,Ceramics and Composites,Electronic, Optical and Magnetic Materials,Catalysis

Link

http://pubs.rsc.org/en/content/articlepdf/2019/CC/C9CC00328B

Reference36 articles.

1. Multifaceted Roles of Disulfide Bonds. Peptides as Therapeutics

2. Discovery, Synthesis, and Structure–Activity Relationships of Conotoxins

3. Structure of the insulin receptor–insulin complex by single-particle cryo-EM analysis

4. Structure-Based Design of Inhibitors of Protein-Protein Interactions: Mimicking Peptide Binding Epitopes

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