Effects of functional groups on the structure, physicochemical and biological properties of mesoporous bioactive glass scaffolds

2015 ◽  
Vol 3 (8) ◽  
pp. 1612-1623 ◽  
Author(s):  
Shichang Zhao ◽  
Jianhua Zhang ◽  
Min Zhu ◽  
Yadong Zhang ◽  
Zhongtang Liu ◽  
...  

Functionalization of biomaterials with specific functional groups is one of the most straightforward strategies to induce specific cell responses to biomaterials.

RSC Advances ◽  
2014 ◽  
Vol 4 (43) ◽  
pp. 22678-22687 ◽  
Author(s):  
Qing Hu ◽  
Yuli Li ◽  
Guohou Miao ◽  
Naru Zhao ◽  
Xiaofeng Chen

Monodispersed mesoporous bioactive glass sub-micron spheres with a controllable size and good biocompatibility were fabricated by an improved sol–gel method.


Nanomaterials ◽  
2020 ◽  
Vol 10 (10) ◽  
pp. 1943 ◽  
Author(s):  
Yeonju Choi ◽  
Woogyeong Sun ◽  
Yeon Kim ◽  
In-Ryoung Kim ◽  
Mi-Kyung Gong ◽  
...  

The purpose of this study was to assess the effects in the dentin bond strength of dental adhesives (DAs) and biological effects using zinc (Zn)-doped mesoporous bioactive glass nanoparticles (MBN-Zn). Synthesized MBN and MBN-Zn were characterized by scanning electron microscopy (SEM), X-ray diffraction and the Brunauer, Emmett and Teller (BET) method. The matrix metalloproteinases (MMP) inhibition effects of DA-MBN and DA-MBN-Zn were analyzed. The microtensile bond strength (MTBS) test was conducted before and after thermocycling to investigate the effects of MBN and MBN-Zn on the MTBS of DAs. The biological properties of DA-MBN and DA-MBN-Zn were analyzed with human dental pulp stem cells (hDPSCs). Compared with the DA, only the DA-1.0% MBN and DA-1.0% MBN-Zn exhibited a statistically significant decrease in MMP activity. The MTBS values after thermocycling were significantly increased in DA-1.0% MBN and DA-1.0% MBN-Zn compared with the DA (p < 0.05). It was confirmed via the MTT assay that there was no cytotoxicity for hDPSCs at 50% extract. In addition, significant increases in the alkaline phosphatase activity and Alizarin Red S staining were observed only in DA-1.0%MBN-Zn. These data suggest the 1.0% MBN and 1.0% MBN-Zn enhance the remineralization capability of DAs and stabilize the long-term MTBS of DAs by inhibiting MMPs.


2014 ◽  
Vol 50 (4) ◽  
pp. 1794-1804 ◽  
Author(s):  
Asma Tufail Shah ◽  
Quratul Ain ◽  
Aqif Anwar Chaudhry ◽  
Ather Farooq Khan ◽  
Bushra Iqbal ◽  
...  

2013 ◽  
Vol 1 (9) ◽  
pp. 1279 ◽  
Author(s):  
Yufang Zhu ◽  
Fangjian Shang ◽  
Bo Li ◽  
Yu Dong ◽  
Yunfei Liu ◽  
...  

Biomolecules ◽  
2021 ◽  
Vol 11 (7) ◽  
pp. 1003
Author(s):  
Zhuning Wu ◽  
Stefanie H. Korntner ◽  
Jos Olijve ◽  
Anne Maria Mullen ◽  
Dimitios I. Zeugolis

In the medical device sector, bloom index and residual endotoxins should be controlled, as they are crucial regulators of the device’s physicochemical and biological properties. It is also imperative to identify a suitable crosslinking method to increase mechanical integrity, without jeopardising cellular functions of gelatin-based devices. Herein, gelatin preparations with variable bloom index and endotoxin levels were used to fabricate non-crosslinked and polyethylene glycol succinimidyl glutarate crosslinked gelatin scaffolds, the physicochemical and biological properties of which were subsequently assessed. Gelatin preparations with low bloom index resulted in hydrogels with significantly (p < 0.05) lower compression stress, elastic modulus and resistance to enzymatic degradation, and significantly higher (p < 0.05) free amine content than gelatin preparations with high bloom index. Gelatin preparations with high endotoxin levels resulted in films that induced significantly (p < 0.05) higher macrophage clusters than gelatin preparations with low endotoxin level. Our data suggest that the bloom index modulates the physicochemical properties, and the endotoxin content regulates the biological response of gelatin biomaterials. Although polyethylene glycol succinimidyl glutarate crosslinking significantly (p < 0.05) increased compression stress, elastic modulus and resistance to enzymatic degradation, and significantly (p < 0.05) decreased free amine content, at the concentration used, it did not provide sufficient structural integrity to support cell culture. Therefore, the quest for the optimal gelatin crosslinker continues.


Sign in / Sign up

Export Citation Format

Share Document