Preparation and Characterization of Antibacterial Porcine Acellular Dermal Matrices with High Performance.

Infection is a common complication in the process of wound management. An ideal wound dressing is supposed to reduce or even prevent the infection while promoting wound healing. A porcine acellular dermal matrix (pADM) has been already used as a wound dressing in clinic due to its capacity to accelerate wound healing. However, not only is pure pADM not antibacterial, its mechanical properties are poor. In this study, an antibacterial pADM with good performance was prepared by adding two natural products as modifiers, quercetin (QCT) and tea tree oil (TTO). The result of Fourier-transform infrared (FTIR) proved that the addition of modifiers did not break the natural triple-helical structure of collagen. Meanwhile, the results of differential scanning calorimetry (DSC), thermogravimetric analysis (TG), mechanic experiment, and enzymatic degradation demonstrated that pADM handled with QCT and TTO (termed QCT-TTO-pADM) had better thermal stability, mechanical strength, and resistance to enzymatic degradation than pADM. Meanwhile, QCT-TTO-pADM had excellent antibacterial activity and showed an antibacterial rate of over 80%. Furthermore, in the cytocompatibility analysis, QCT-TTO-pADM had no side effects on the adhesion, growth, and proliferation of fibroblasts. QCT-TTO-pADM could even accelerate wound healing more efficiently than pADM and glutaraldehyde-modified pADM (GA-pADM). In conclusion, QCT-TTO-pADM was a potential antibacterial wound dressing with good performance.

Feasibility study of the natural derived chitosan dialdehyde for chemical modification of collagen.

The aim of this study is to evaluate the chemical crosslinking effects of the natural derived chitosan dialdehyde (OCS) on collagen. Fourier transform infrared (FTIR) spectroscopy, differential scanning calorimetry (DSC) and circular dichroism (CD) measurements suggest that introducing OCS might not destroy the natural triple helix conformation of collagen but enhance the thermal-stability of collagen. Meanwhile, a denser fibrous network of cross-linked collagen is observed by atomic force microscopy. Further, scanning electron microscopy (SEM) and aggregation kinetics analysis confirm that the fibrillation process of collagen advances successfully and OCS could lengthen the completion time of collagen fibrillogenesis but raise the reconstitution rate of collagen fibrils or microfibrils. Besides, the cytocompatibility analysis implies that when the dosage of OCS is less than 15%, introducing OCS into collagen might be favorable for the cell's adhesion, growth and proliferation. Taken as a whole, the present study demonstrates that OCS might be an ideal crosslinker for the chemical fixation of collagen.