Collagen type I, commonly derived from xenogenic sources, is extensively used as a biomaterial for tissue engineering applications. However, the use of xenogenic collagen is typically associated with species specific variation in mechanical, structural, and biological properties that are known to influence cellular response and remodeling. In addition, immunological complications and risks of disease transmission are also major concerns. The goal of this study is to characterize a new xeno-free human skin-derived collagen and assess its applicability as a bioink for cell-laden 3 D bioprinting. Four different concentrations of human collagen (i.e., 0.5 mg/mL, 1 mg/mL, 3 mg/mL and 6 mg/mL) were employed for the synthesis of collagen hydrogels. In addition, bovine collagen was used as a xenogenic control. Results from SDS-PAGE analysis showed the presence of α1, α2, and β chains, confirming that the integrity of type I human collagen is maintained post isolation. Polymerization rate and compressive modulus increased significantly with increase in the concentration of human collagen. When comparing two different sources of collagen, the polymerization rate of xenogenic collagen was significantly faster (p < 0.05) than human collagen while the compressive modulus was comparable. Raman spectroscopy showed a large peak in the Amide I band around 1600 cm⁻¹, indicating a dense and supraorganized fibrillar structure in human collagen hydrogels. Conversely, Amide I band intensity for xenogenic collagen was comparable to that of Amide II and Amide III bands. Further, the use of 6 mg/mL human collagen as a bioink yielded 3 D printed constructs with high shape fidelity and cell viability. On the other hand, xenogenic collagen failed to yield stable 3 D printed constructs. Together, the results from this study provides an impetus for using human-derived collagen as a viable alternative to xenogenic sources for 3 D bioprinting of clinically relevant scaffolds for tissue engineering applications.

I 型胶原蛋白通常来自异种来源，被广泛用作组织工程应用的生物材料。然而，异种胶原蛋白的使用通常与已知会影响细胞反应和重塑的机械、结构和生物学特性的物种特异性变化有关。此外，免疫并发症和疾病传播风险也是主要问题。本研究的目的是表征一种新的无异种人体皮肤衍生胶原蛋白，并评估其作为载有细胞的 3D 生物打印的生物墨水的适用性。四种不同浓度的人胶原蛋白（即0.5 mg/mL、1 mg/mL、3 mg/mL和6 mg/mL）用于合成胶原蛋白水凝胶。此外，牛胶原蛋白用作异种对照。SDS-PAGE 分析结果显示存在 α1、α2 和 β 链，证实 I 型人胶原蛋白的完整性在分离后得以保持。随着人体胶原蛋白浓度的增加，聚合速率和压缩模量显着增加。当比较两种不同来源的胶原蛋白时，异种胶原蛋白的聚合速率明显快于人胶原蛋白（p < 0.05），而压缩模量相当。拉曼光谱显示在 1600 cm 附近的 Amide I 波段有一个大峰 异种胶原蛋白的聚合速率明显快于人胶原蛋白（p < 0.05），而压缩模量相当。拉曼光谱显示在 1600 cm 附近的 Amide I 波段有一个大峰 异种胶原蛋白的聚合速率明显快于人胶原蛋白（p < 0.05），而压缩模量相当。拉曼光谱显示在 1600 cm 附近的 Amide I 波段有一个大峰^-1，表明人胶原水凝胶中有致密且超组织的纤维状结构。相反，异种胶原的酰胺 I 条带强度与酰胺 II 和酰胺 III 条带的强度相当。此外，使用 6 mg/mL 人类胶原蛋白作为生物墨水产生了具有高形状保真度和细胞活力的 3D 打印结构。另一方面，异种胶原蛋白未能产生稳定的 3D 打印结构。总之，这项研究的结果为使用人源胶原蛋白作为异种来源的可行替代品提供了动力，用于组织工程应用的临床相关支架的 3D 生物打印。