Affiliations: Department of Medicine, Baylor College of Medicine, Houston, TX 77030, USA | Department of Orthopedic Surgery, Baylor College of Medicine, Houston, TX 77030, USA
Note: [] Corresponding author: Zong-Ping Luo, Baylor College of Medicine, Department of Orthopedic Surgery 6550 Fannin, Suite 451, Houston, TX 77030, USA. Tel.: +1 713 986 5522; Fax: +1 713 986 5519; E-mail: luo@bcm.tmc.edu.
Abstract: An understanding of collagen ultrastructure is very important for designing biopolymers mimicking collagen functions in tissue engineering, or for diagnosing abnormal collagen structure in clinical study. The present study examined formation of a large population of type I collagen single fibrils under different buffer compositions and temperatures. Fibril structures were investigated by dark-field microscopy and atomic force microscopy (AFM). In the phosphate buffered saline (PBS) buffer, the average lengths of single fibrils were 4.8±2.2, 5.0±1.9 and 9.2±5.0 μm for 37°C, 33°C and 29°C, respectively. The differences were significant (P<0.05) between 37°C and 29°C and between 33°C and 29°C. In the sodium phosphate (SP) buffer, the average lengths of single fibrils were 10.6±5.4, 11.1±4.5 and 19.6±11.7 μm for 37°C, 33°C and 29°C, respectively. Similarly, the differences were significant (P<0.05) between 37°C and 29°C and between 33°C and 29°C. While at the same temperature, the average lengths of single fibrils differed significantly (P<0.05) between PBS and SP buffers. Single fibrils formed in SP buffer were found to have greater average length than those formed in PBS buffer.
Keywords: Type I collagen single fibril, dark-field microscopy, atomic force microscopy, buffer compositions, temperature
