Silk fibroin-derived polypeptides additives to promote hydroxyapatite nucleation in dense collagen hydrogels.
Animals
Biocompatible Materials
/ chemistry
Body Fluids
Bombyx
Bone Substitutes
Collagen
/ chemistry
Durapatite
/ chemistry
Fibroins
/ chemistry
Hydrogels
/ chemistry
Hydrogen-Ion Concentration
Microscopy, Electron, Scanning
Particle Size
Peptides
/ chemistry
Spectroscopy, Fourier Transform Infrared
Temperature
Tissue Engineering
/ methods
Tissue Scaffolds
/ chemistry
X-Ray Diffraction
Journal
PloS one
ISSN: 1932-6203
Titre abrégé: PLoS One
Pays: United States
ID NLM: 101285081
Informations de publication
Date de publication:
2019
2019
Historique:
received:
29
09
2018
accepted:
24
06
2019
entrez:
16
7
2019
pubmed:
16
7
2019
medline:
10
3
2020
Statut:
epublish
Résumé
Silk fibroin-derived polypeptides (FDPs) are polypeptides resulting from the enzymatic separation of the hydrophobic crystalline (Cp) and hydrophilic electronegative amorphous (Cs) components of silk fibroin (SF). The role of these polypeptides in promoting the nucleation of hydroxyapatite (HA) has been previously investigated, yet is still not fully understood. Here we study the potential of HA mineralization via FDPs incorporated at 1:10, 1:2 and 1:1 in a plastically compressed (PC) and dense collagen (DC) scaffold. Scaffolds were immersed in simulated body fluid (SBF) at physiological conditions (pH = 7.4, 37°C) to promote biomineralization. The effect of Cs and Cp to promote HA nucleation was investigated at different time points, and compared to pure DC scaffolds. Characterization of Cs and Cp fragments using Liquid Chromatography-Mass Spectrometry (LCMS) showed little difference in the amino acid composition of the FDPs. Results obtained in vitro using Attenuated Total Reflectance Fourier Transform Infrared Spectroscopy (ATR-FTIR), Scanning Electron Microscopy (SEM) X-Ray Diffraction (XRD) and mass analysis showed little difference between scaffolds that incorporated Cs, Cp, and DC hydrogels. These results demonstrated that silk FDPs incorporation are not yet suitable to promote HA nucleation in vivo without further refining the collagen-FDP system.
Identifiants
pubmed: 31306436
doi: 10.1371/journal.pone.0219429
pii: PONE-D-18-27511
pmc: PMC6629059
doi:
Substances chimiques
Biocompatible Materials
0
Bone Substitutes
0
Hydrogels
0
Peptides
0
Collagen
9007-34-5
Fibroins
9007-76-5
Durapatite
91D9GV0Z28
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e0219429Déclaration de conflit d'intérêts
The authors have declared that no competing interests exist.
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