Mechanical and structural responses of silk fibroin scaffolds to MechanoCulture T6® bioreactor loading and enzymatic degradation.

Λεπτομέρειες βιβλιογραφικής εγγραφής
Τίτλος: Mechanical and structural responses of silk fibroin scaffolds to MechanoCulture T6® bioreactor loading and enzymatic degradation.
Συγγραφείς: Aikman EL; Department of Chemical Engineering, University of Florida, Gainesville, FL, USA., Byron LY; Department of Chemistry, Butler Polymer Research Laboratory, Center for Macromolecular Science & Engineering, University of Florida, Gainesville, FL, USA., Beshay CA; J. Crayton Pruitt Family Department of Biomedical Engineering, Gainesville, FL, USA., Urbina JA; Department of Mechanical and Aerospace Engineering, University of Florida, Gainesville, FL, USA., Davis AN; Department of Chemistry, Butler Polymer Research Laboratory, Center for Macromolecular Science & Engineering, University of Florida, Gainesville, FL, USA., Evans AM; Department of Chemistry, Butler Polymer Research Laboratory, Center for Macromolecular Science & Engineering, University of Florida, Gainesville, FL, USA; Department of Materials Science and Engineering, University of Florida, Gainesville, FL, USA., Stoppel WL; Department of Chemical Engineering, University of Florida, Gainesville, FL, USA; J. Crayton Pruitt Family Department of Biomedical Engineering, Gainesville, FL, USA. Electronic address: whitney.stoppel@ufl.edu.
Πηγή: Journal of the mechanical behavior of biomedical materials [J Mech Behav Biomed Mater] 2026 Aug; Vol. 180, pp. 107474. Date of Electronic Publication: 2026 May 25.
Τύπος έκδοσης: Journal Article
Γλώσσα: English
Στοιχεία περιοδικού: Publisher: Elsevier Country of Publication: Netherlands NLM ID: 101322406 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1878-0180 (Electronic) Linking ISSN: 18780180 NLM ISO Abbreviation: J Mech Behav Biomed Mater Subsets: MEDLINE
Imprint Name(s): Original Publication: Amsterdam : Elsevier
Ιατρικοί όροι (MeSH): Fibroins*/chemistry , Fibroins*/metabolism , Tissue Scaffolds*/chemistry , Bioreactors* , Mechanical Phenomena*, Biocompatible Materials/chemistry ; Animals ; Materials Testing ; Bombyx ; Stress, Mechanical
Περίληψη: Silk fibroin is a semicrystalline biopolymer derived from Bombyx mori cocoons that can be fabricated into various biomaterials including aligned porous scaffolds. Silk fibroin is an ideal biomaterial polymer due to its tunable pore sizes and mechanical properties, which match those of aligned soft tissues, as well as its biocompatibility, non-toxic effects, and tunable degradation. This in vitro platform was developed from ice-templated anisotropic silk fibroin scaffolds toward modeling aligned soft tissues using mechanical loading via a bioreactor. Different scaffold fabrication post-lyophilization parameters gave varied self-assembly of the amino acid building blocks of silk fibroin, as explored through crystalline structures and in vitro degradation. X-ray scattering revealed a longer-range order of the crystalline domains when scaffolds were subjected to slower post-lyophilization processing. This structural difference also manifested in different rates of enzymatic degradation, where protease XIV was able to cleave the amorphous regions between smaller crystalline domains more rapidly. MechanoCulture T6 bioreactor stimulation occurred for 5, 10, or 25 days at 1 Hz, 10% strain for 30 min with 11.5 h of rest periods to mimic skeletal muscle stimulation for hypertrophy. Hydrated uniaxial rheology was used to assess Young's modulus (E), ultimate tensile stress (UTS), and strain at break. The mechanical properties and internal porosity were found to be independent of storage, loading, and time. Scanning electron microscopy (SEM) and nano-computed tomography (nano-CT) showed minimal differences in scaffold structural properties after bioreactor loading. Ice-templated silk fibroin scaffolds were shown to be suitable for new approach methods requiring mechanical stimulation.
(Copyright © 2026. Published by Elsevier Ltd.)
Competing Interests: Declaration of competing interest The authors declare the following financial interests/personal relationships which may be considered as potential competing interests: Whitney L. Stoppel reports financial support was provided by National Institute of General Medical Sciences. Elizabeth L Aikman reports financial support was provided by National Institute of General Medical Sciences. Llia Y. Byron reports financial support was provided by National Institute of General Medical Sciences. Cathrine A. Beshay reports financial support was provided by National Institute of General Medical Sciences. Jacob A. Urbina reports financial support was provided by National Institute of General Medical Sciences. Austin M. Evans reports financial support was provided by DEVCOM ARO DURIP. Elizabeth L. Aikman reports financial support was provided by National Science Foundation Division of Graduate Education. If there are other authors, they declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
Contributed Indexing: Keywords: Crystallinity; Degradation; Dynamic mechanics; Ice-templating; Silk fibroin
Substance Nomenclature: 9007-76-5 (Fibroins)
0 (Biocompatible Materials)
Entry Date(s): Date Created: 20260602 Date Completed: 20260613 Latest Revision: 20260613
Update Code: 20260613
DOI: 10.1016/j.jmbbm.2026.107474
PMID: 42229073
Βάση Δεδομένων: MEDLINE