Comparison of the structure and function of a chimeric peptide modified titanium surface-Reference-Cited by-同舟云学术

Comparison of the structure and function of a chimeric peptide modified titanium surface

Published:2019 Issue:45 Volume:9 Page:26276-26282
ISSN:2046-2069
Container-title:RSC Advances
language:en
Short-container-title:RSC Adv.

Author:

Gong Lei¹²³⁴⁵,Geng Hongjuan⁶⁷⁸,Zhang Xi⁹¹⁰¹¹⁸^ORCID,Gao Ping⁹¹⁰¹¹⁸

Affiliation:

1. Department of Esophageal Cancer

2. Tianjin's Clinical Research Center for Cancer

3. Key Laboratory of Cancer Prevention and Therapy

4. National Clinical Research Center for Cancer

5. Tianjin Medical University Cancer Institute and Hospital

6. Department of Stomatology

7. Tianjin

8. PR China

9. School and Hospital of Stomatology

10. Tianjin Medical University

11. Tianjin 300070

Abstract

The antimicrobial activity of Tyr structure in hBD3-3 is stronger than that of the α-helix structure in multifunctional chimeric peptides. Rigid connections avoid functional domain changes. Endogenous peptide fragments on a Ti surface could reduce peri-implant diseases.

Funder

National Natural Science Foundation of China

Wu Jieping Medical Foundation

Natural Science Foundation of Tianjin City

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemical Engineering,General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2019/RA/C9RA05127A

Reference40 articles.

1. Peri-implant diseases and conditions: Consensus report of workgroup 4 of the 2017 World Workshop on the Classification of Periodontal and Peri-Implant Diseases and Conditions