Probing the alignment-dependent mechanical behaviors and time-evolutional aligning process of collagen scaffolds

Zhai, Chenxi; Sullivan, Patrick A.; Martin, Cassandra; Shi, Haoyuan; Deravi, Leila F.; Yeo, Jingjie

doi:10.1039/d2tb01360f

Cited by 3 publications

(1 citation statement)

References 42 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In comparison to the blank and grass carp group, quantitative results revealed that the migration ratio reached the peak under cross‐link (10%), while the migration behaviors decreased when the EDC/NHS cross‐link concentration reached to 50% or 100% (Figure 3D). Previous reports demonstrated that cross‐link could regulate the mechanical properties of collagen, [ 23 ] and stiffness favors the migration of cells. [ 24 ] Then we speculated that the migration behavior in the cross‐link condition (Figure 3D) was mainly controlled by these two factors.…”

Section: Resultsmentioning

confidence: 99%

Fish‐Derived Collagen: A Promising Biomaterial for Regulating the Migration Behavior of MCF‐7 Cells

Zhu,

Xiao,

Zhu

et al. 2024

Adv Eng Mater

View full text Add to dashboard Cite

Uncontrollable migration of cancer cells is one of the reasons for the poor prognosis. The interaction between collagen and cellular processes is usually dominated by the full triple‐helix structure of collagen. However, it remains to be explored how the collagen configuration affects the migration behaviors of cancer cells. MCF‐7 cells were chosen to study this relationship. Meanwhile, the grass carp is one of the representative fish species in Hubei, and is virtually unaffected by zoonotic diseases. Therefore, grass carp‐derived collagen was prepared and used to modulate the migration behaviors. Collagen sample was pretreated via several procedures including hydrothermal process, EDC/NHS, respectively. The underlying mechanisms affecting migration behavior are explored by tuning the degree of denaturation, assembly states, and cross‐linking conditions of collagen. Results demonstrate that moderate cross‐linking and assembly contribute to the migration processes, while denaturation significantly suppresses migration. Of particular note is the positive correlation of F‐actin expression levels with these phenomena. More importantly, the hydrophilic and hydrophobic properties of collagen surface also affect the migration process. In summary, our study may provide insights to flexibly tune the migration behavior of cancer cells, which may be promising in inhibiting tumor metastasis.This article is protected by copyright. All rights reserved.

show abstract

Section: Resultsmentioning

confidence: 99%

Fish‐Derived Collagen: A Promising Biomaterial for Regulating the Migration Behavior of MCF‐7 Cells

Zhu,

Xiao,

Zhu

et al. 2024

Adv Eng Mater

View full text Add to dashboard Cite

show abstract

Recent Advances on Collagen Biomaterial: From Extraction, Cross-Linking to Tissue Regeneration

Zhu,

Yu,

et al. 2024

Polymer Reviews

View full text Add to dashboard Cite

Computational and Experimental Characterization of Aligned Collagen across Varied Crosslinking Degrees

Lin,

Patrawalla,

Zhai

et al. 2024

Micromachines

View full text Add to dashboard Cite

Collagen-based scaffolds have been widely used in tissue engineering. The alignment of collagen fibers and the degree of crosslinking in engineering tissue scaffolds significantly affect cell activity and scaffold stability. Changes in microarchitecture and crosslinking degree also impact the mechanical properties of collagen scaffolds. A clear understanding of the effects of collagen alignment and crosslinking degrees can help properly control these critical parameters for fabricating collagen scaffolds with desired mechanical properties. In this study, combined uniaxial mechanical testing and finite element method (FEM) were used to quantify the effects of fiber alignment and crosslinking degree on the mechanical properties of collagen threads. We have fabricated electrochemically aligned collagen (ELAC) and compared it with randomly distributed collagen at varying crosslinking degrees, which depend on genipin concentrations of 0.1% or 2% for crosslinking durations of 1, 4, and 24 h. Our results indicate that aligned collagen fibers and higher crosslinking degree contribute to a larger Young’s modulus. Specifically, aligned fiber structure, compared to random collagen, significantly increases Young’s modulus by 112.7% at a 25% crosslinking degree (0.1% (4 h), i.e., 0.1% genipin concentration with a crosslinking duration of 4 h). Moreover, the ELAC Young’s modulus increased by 90.3% as the crosslinking degree doubled by changing the genipin concentration from 0.1% to 2% with the same 4 h crosslinking duration. Furthermore, verified computational models can predict mechanical properties based on specific crosslinking degrees and fiber alignments, which facilitate the controlled fabrication of collagen threads. This combined experimental and computational approach provides a systematic understanding of the interplay among fiber alignment, crosslinking parameters, and mechanical performance of collagen scaffolds. This work will enable the precise fabrication of collagen threads for desired tissue engineering performance, potentially advancing tissue engineering applications.

show abstract

Probing the alignment-dependent mechanical behaviors and time-evolutional aligning process of collagen scaffolds

Abstract: Efficiently manipulating and reproducing the collagen (COL) alignment in vitro remains challenging because many of the fundamental mechanisms underlying and guiding the alignment process are not known. We reconcile experiments...

Cited by 3 publications

References 42 publications

Fish‐Derived Collagen: A Promising Biomaterial for Regulating the Migration Behavior of MCF‐7 Cells

Fish‐Derived Collagen: A Promising Biomaterial for Regulating the Migration Behavior of MCF‐7 Cells

Recent Advances on Collagen Biomaterial: From Extraction, Cross-Linking to Tissue Regeneration

Computational and Experimental Characterization of Aligned Collagen across Varied Crosslinking Degrees

Contact Info

Product

Resources

About