Premium
Silk‐Inspired β‐Peptide Materials Resist Fouling and the Foreign‐Body Response
Author(s) -
Zhang Donghui,
Chen Qi,
Zhang Wenjing,
Liu Hengjiang,
Wan Jianglin,
Qian Yuxin,
Li Bing,
Tang Songchao,
Liu Yu,
Chen Shengfu,
Liu Runhui
Publication year - 2020
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.202000416
Subject(s) - self healing hydrogels , silk , chemistry , protein adsorption , amino acid , peptide , branching (polymer chemistry) , dipeptide , serine , biophysics , materials science , polymer chemistry , adsorption , biochemistry , phosphorylation , organic chemistry , biology , composite material
The functions of implants like medical devices are often compromised by the host's foreign‐body response (FBR). Herein, we report the development of low‐FBR materials inspired by serine‐rich sericin from silk. Poly‐β‐homoserine (β‐HS) materials consist of the hydrophilic unnatural amino acid β‐homoserine. Self‐assembled monolayers (SAMs) of β‐HS resist adsorption by diverse proteins, as well as adhesion by cells, platelets, and diverse microbes. Experiments lasting up to 3 months revealed that, while implantation with control PEG hydrogels induced obvious inflammatory responses, collagen encapsulation, and macrophage accumulation, these responses were minimal with β‐HS hydrogels. Strikingly, the β‐HS hydrogels induce angiogenesis in implant‐adjacent tissues. Molecular dynamics simulations indicated that the low FBR performance of β‐HS results from what we term “dual hydrogen bonding hydration”, wherein both the backbone amide groups and the sidechain hydroxyl groups of β‐HS undergo hydration.