Applications and degradation of proteins used as tissue engineering materials
Open accessAbstract
This article provides an up-to-date review on the applications of natural polymers, i.e., proteins, as materials for tissue engineering. Proteins are one of the important candidates for tissue engineering materials based on their superior biocompatibility, biodegradation, bioresorbability, and so on. However, their inferior mechanical properties limit their broad application. Currently-available proteins for application in tissue engineering or drug delivery systems, such as fibrin, collagen, zein, silk fibroin, keratin, casein and albumin, and the biodegradation of tissue-engineered substitutes based on proteins are presented. Techniques of scaffold fabrication are also mentioned. Problems and future possibilities for development of protein-based tissue-engineered substitutes are also introduced in this review.
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When silk fibroin is degraded, the resulting amino acids can be taken up outside the body without significant toxicity to cells.
“When silk fibroin is degraded, the resulting amino acids can be taken up outside the body without significant toxicity to the cells [29], a property that is favorable for biomedical applications.”
From Recent Advances in Silk Fibroin-Based Composites for Bone Repair Applications: A Review (2025) · cites this paper as [29]
The Introduction (page unavailable) says protein degradation produces amino acids that can be resorbed as nutrients, and §2.4 describes silk fibroin as biocompatible and biodegradable. Neither passage establishes that amino acids from degraded silk fibroin are taken up outside the body without significant toxicity to cells. (LLM, conf=0.84)
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Flagged first, then by citations
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Recent Advances in Silk Fibroin-Based Composites for Bone Repair Applications: A Review
Zhu, S., Zhang, Q., Xu, X., Liu, Z., Cheng, G., Long, D., Cheng, L., & Dai, F. (2025) · Polymers · doi:10.3390/polym17060772 · Cited by 36 · see citing works
“When silk fibroin is degraded, the resulting amino acids can be taken up outside the body without significant toxicity to the cells [29], a property that is favorable for biomedical applications.”
- Authors
- Wang, H.-J., Di, L., Ren, Q.-S., & Wang, J.-Y.
- Affiliations
- Shanghai Jiao Tong University (CN)
- Biomedical Engineering, School of Life Science and Biotechnology, Shanghai Jiao Tong University, 800 Dongchuan Road, Shanghai 200240, China
- Corresponding author
- Wang, Jin-Ye
- Venue
- Materials
- Publisher
- MDPI AG
- Published
- 2009-05-26
- Volume
- 2
- Issue
- 2
- Pages
- 613-635
- ISSN
- 1996-1944 (ISSN-L)
- PMC
- PMC5445712
- OpenAlex
- W2044067048
- Cited by
- 62
- References
- 146
- Citations by year
- 2026: 1 · 2025: 6 · 2024: 1 · 2023: 7 · 2022: 7 · 2021: 5 · 2020: 5 · 2019: 3 · 2018: 7 · 2017: 9 · 2016: 3 · 2015: 3 · 2014: 3 · 2013: 1 · 2012: 1
- FWCI
- 0.15
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Materials (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Topics
- Physical Sciences › Materials Science › Biomaterials › Silk-based biomaterials and applications
- Physical Sciences › Materials Science › Biomaterials › Collagen: Extraction and Characterization
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Medicine › Hydrogels: synthesis, properties, applications
- Keywords
- protein-based biomaterials, tissue engineering scaffolds, biodegradation, biocompatibility, fibrin, collagen, zein, silk fibroin, keratin, casein, albumin, drug delivery systems, scaffold fabrication, protein mechanical properties
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