Native human collagen type I provides a viable physiologically relevant alternative to xenogeneic sources for tissue engineering applications: A comparative in vitro and in vivo study

• Published in: Journal of biomedical materials research. Part B, Applied biomaterials Vol. 110; no. 10; pp. 2323 - 2337
• Main Authors: Baltazar, Tânia, Kajave, Nilabh S., Rodriguez, Marco, Chakraborty, Srija, Jiang, Bo, Skardal, Aleksander, Kishore, Vipuil, Pober, Jordan S., Albanna, Mohammad Z.
• Format: Journal Article
• Language: English
• Published: Hoboken, USA John Wiley & Sons, Inc 01.10.2022; Wiley Subscription Services, Inc
• Subjects: 3D construct; Amino acid composition; Amino acids; Animals; Biological properties; Biomedical materials; cancer modeling; Cell culture; Chemical properties; Chemotherapy; Collagen; Collagen - chemistry; Collagen - pharmacology; collagen type I; Collagen Type I - chemistry; Collagen Type I - pharmacology; Drug screening; Extracellular Matrix - chemistry; Human performance; Humans; hydrogel; Hydrogels; Hydrogels - chemistry; In vivo methods and tests; Materials research; Materials science; Medicine; Modulus of elasticity; Physical properties; Production methods; Rats; Regenerative medicine; Skin; Substrates; Swelling ratio; Tissue engineering; Tissue Engineering - methods; Tissue Scaffolds - chemistry; Tumors; xeno; collagen type I; cancer modeling; 3D construct; hydrogel; xeno
• ISSN: 1552-4973; 1552-4981
• DOI: 10.1002/jbm.b.35080

Xenogeneic sources of collagen type I remain a common choice for regenerative medicine applications due to ease of availability. Human and animal sources have some similarities, but small variations in amino acid composition can influence the physical properties of collagen, cellular response, and tissue remodeling. The goal of this work is to compare human collagen type I‐based hydrogels versus animal‐derived collagen type I‐based hydrogels, generated from commercially available products, for their physico‐chemical properties and for tissue engineering and regenerative medicine applications. Specifically, we evaluated whether the native human skin type I collagen could be used in the three most common research applications of this protein: as a substrate for attachment and proliferation of conventional 2D cell culture; as a source of matrix for a 3D cell culture; and as a source of matrix for tissue engineering. Results showed that species and tissue specific variations of collagen sources significantly impact the physical, chemical, and biological properties of collagen hydrogels including gelation kinetics, swelling ratio, collagen fiber morphology, compressive modulus, stability, and metabolic activity of hMSCs. Tumor constructs formulated with human skin collagen showed a differential response to chemotherapy agents compared to rat tail collagen. Human skin collagen performed comparably to rat tail collagen and enabled assembly of perfused human vessels in vivo. Despite differences in collagen manufacturing methods and supplied forms, the results suggest that commercially available human collagen can be used in lieu of xenogeneic sources to create functional scaffolds, but not all sources of human collagen behave similarly. These factors must be considered in the development of 3D tissues for drug screening and regenerative medicine applications.