Physical characterization of succinylated type I collagen by Raman spectra and MALDI-TOF/MS and in vitro evaluation for biomedical applications
✍ Scribed by Ramadhar Kumar; R. Sripriya; S. Balaji; M. Senthil Kumar; P.K. Sehgal
- Book ID
- 103839836
- Publisher
- Elsevier Science
- Year
- 2011
- Tongue
- English
- Weight
- 956 KB
- Volume
- 994
- Category
- Article
- ISSN
- 0022-2860
No coin nor oath required. For personal study only.
✦ Synopsis
In this study, we report on physical and in vitro biological characterization of succinylated collagen (SC). SC was prepared by succinylation of type I bovine tendon collagen. SC swells and dissolves in physiological pH buffers (pH 7.4) Biocompatibility of SC to collagen for fibroblasts was comparable but L6 myoblasts showed pronounced proliferation and differentiation with SC. Using the MALDI-TOF/MS technique, SC was found with increased molecular mass by 16,359Da per molecule which corresponds to about 54 succinyl groups covalently linked to the collagen strand. Raman spectroscopy revealed the retention of triple helical structure conformation in the presence of linked succinyl groups. New peaks near 1737, 1675 and 1420cm−1 and decreased intensities near 2440 and 488cm−1 provides the most convenient marker bands for succinylation of collagen. The intense band regions near 2856–2934, 2724, and 1445cm−1 also confirms the existence of succinyl groups.