Details
| Original language | English |
|---|---|
| Pages (from-to) | 4190-4200 |
| Number of pages | 11 |
| Journal | RSC Advances |
| Volume | 10 |
| Issue number | 8 |
| Early online date | 24 Jan 2020 |
| Publication status | Published - 2020 |
| Externally published | Yes |
Abstract
Fibrin is a well-known tool in tissue engineering, but the structure of its modifications created to improve its properties remains undiscussed despite its importance, e.g. in designing biomaterials that ensure cell migration and lumenogenesis. We sought to uncover the structural aspects of PEGylated fibrin hydrogels shown to contribute to angiogenesis. The analysis of the small-angle X-ray scattering (SAXS) data and ab initio modeling revealed that the PEGylation of fibrinogen led to the formation of oligomeric species, which are larger at a higher PEG : fibrinogen molar ratio. The improvement of optical properties was provided by the decrease in aggregates' sizes and also by retaining the bound water. Compared to the native fibrin, the structure of the 5 : 1 PEGylated fibrin gel consisted of homogenously distributed flexible fibrils with a smaller space between them. Moreover, as arginylglycylaspartic acid (RGD) sites may be partly bound to PEG-NHS or masked because of the oligomerization, the number of adhesion sites may be slightly reduced that may provide the better cell migration and formation of continuous capillary-like structures.
ASJC Scopus subject areas
- Chemistry(all)
- General Chemistry
- Chemical Engineering(all)
- General Chemical Engineering
Cite this
- Standard
- Harvard
- Apa
- Vancouver
- BibTeX
- RIS
In: RSC Advances, Vol. 10, No. 8, 2020, p. 4190-4200.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Digging deeper
T2 - Structural background of PEGylated fibrin gels in cell migration and lumenogenesis
AU - Shpichka, A. I.
AU - Konarev, P. V.
AU - Efremov, Yu M.
AU - Kryukova, A. E.
AU - Aksenova, N. A.
AU - Kotova, S. L.
AU - Frolova, A. A.
AU - Kosheleva, N. V.
AU - Zhigalina, O. M.
AU - Yusupov, V. I.
AU - Khmelenin, D. N.
AU - Koroleva, A.
AU - Volkov, V. V.
AU - Asadchikov, V. E.
AU - Timashev, P. S.
N1 - Funding Information: This work was supported by the Russian Science Foundation 18-15-00407 (confocal laser scanning microscopy, discussion), Russian academic excellence project 5–100 (atomic force microscopy), Russian Foundation for Basic Research 18-02-00658 (biomechanical properties measurements and analysis) and 17-02-00445 (FT-IR and DSC analysis), and the Ministry of Science and Higher Education within the State assignment FSRC “Crystallography and Photonics” RAS (SAXS, turbidity and SEM analysis). It was performed using the equipment of the Shared Research Centre of FSRC “Crystallography and Photonics” RAS (scanning electron microscopy).
PY - 2020
Y1 - 2020
N2 - Fibrin is a well-known tool in tissue engineering, but the structure of its modifications created to improve its properties remains undiscussed despite its importance, e.g. in designing biomaterials that ensure cell migration and lumenogenesis. We sought to uncover the structural aspects of PEGylated fibrin hydrogels shown to contribute to angiogenesis. The analysis of the small-angle X-ray scattering (SAXS) data and ab initio modeling revealed that the PEGylation of fibrinogen led to the formation of oligomeric species, which are larger at a higher PEG : fibrinogen molar ratio. The improvement of optical properties was provided by the decrease in aggregates' sizes and also by retaining the bound water. Compared to the native fibrin, the structure of the 5 : 1 PEGylated fibrin gel consisted of homogenously distributed flexible fibrils with a smaller space between them. Moreover, as arginylglycylaspartic acid (RGD) sites may be partly bound to PEG-NHS or masked because of the oligomerization, the number of adhesion sites may be slightly reduced that may provide the better cell migration and formation of continuous capillary-like structures.
AB - Fibrin is a well-known tool in tissue engineering, but the structure of its modifications created to improve its properties remains undiscussed despite its importance, e.g. in designing biomaterials that ensure cell migration and lumenogenesis. We sought to uncover the structural aspects of PEGylated fibrin hydrogels shown to contribute to angiogenesis. The analysis of the small-angle X-ray scattering (SAXS) data and ab initio modeling revealed that the PEGylation of fibrinogen led to the formation of oligomeric species, which are larger at a higher PEG : fibrinogen molar ratio. The improvement of optical properties was provided by the decrease in aggregates' sizes and also by retaining the bound water. Compared to the native fibrin, the structure of the 5 : 1 PEGylated fibrin gel consisted of homogenously distributed flexible fibrils with a smaller space between them. Moreover, as arginylglycylaspartic acid (RGD) sites may be partly bound to PEG-NHS or masked because of the oligomerization, the number of adhesion sites may be slightly reduced that may provide the better cell migration and formation of continuous capillary-like structures.
UR - http://www.scopus.com/inward/record.url?scp=85079055565&partnerID=8YFLogxK
U2 - 10.1039/c9ra08169k
DO - 10.1039/c9ra08169k
M3 - Article
AN - SCOPUS:85079055565
VL - 10
SP - 4190
EP - 4200
JO - RSC Advances
JF - RSC Advances
SN - 2046-2069
IS - 8
ER -