Collagen is a principal constituent of the extracellular matrix (ECM) and as such, defines the microenvironmental milieu in which cells reside. In fiber-reinforced musculoskeletal tissues, collagen fibers are highly organized and generate the direction-dependent mechanical properties critical to the function of these structures. Given its primary role, collagen is particularly attractive for tissue engineering (TE) applications where scaffolds are coupled with cells to repair or regenerate damaged tissues. One method for producing collagen-based scaffolds is through electrospinning. This technique yields nano- to micron-scale fibers similar in diameter to those of the native ECM. Towards engineering orthopaedic tissues, methods have been devised to electrospin fibers into aligned arrays that can recapitulate the anisotropy of fiber-reinforced tissues [1]. While a number of polymers have been electrospun, collagen-based scaffolds are especially promising as they provide a biomimetic interface for cell attachment [2]. Numerous investigators have electrospun collagen [3], one major drawback is their inherent instability in aqueous environments. To address this, various crosslinking agents including glutaraldehyde (GA), 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide hydrochloride, and N-hydroxysuccinimide chemistries have been used, but these chemicals often prove cytotoxic or excessively laborious in application [4]. Even with crosslinking, dry as-formed nanofibrous collagen scaffolds with moduli greater than 50MPa diminish by 100-fold with rehydration [5].

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