Characterization Of A New Collagen-Like Protein From Trichodesmium erythraeum.

摘要

In order to meet the exponentially rising demands of collagen in the fields of tissue engineering, cosmetic surgery and drug delivery systems, there is an increasing demand to find novel sources. Recently, an intron-free collagen-like gene found in Trichodesmium erythraeum, a colonial marine cyanobacterium, was reported.;This thesis aims at characterizing this new collagen-like sequence and theoretically comparing it with human collagens (especially type I human collagen) and few other bacterial proteins in terms of amino acid composition, flexibility, hydropathicity and charge density. Enzyme degradation and polarized light microscopy were utilized to support the hypothesis of presence of collagen-like protein in T. erythraeum's cell. The initial step of analysis involved running the blastp algorithm using this new sequence as the query sequence and studying its resemblance to various proteins in RefSeq protein database. Comparison with type I human collagen revealed that the assumed homotrimer molecule of Trichodesmium erythraeum 's collagen-like protein is almost as relatively stable as the former. The alternate flexible and rigid domains in the molecular structure can be predicted to coincide and form a highly flexible fibrillar structure that may aid the aggregates to survive stresses from ocean. It is suggested that this collagen-like protein is primarily responsible for transmission of energy during loading and not as much for storage of elastic energy. This new sequence was found to be highly hydrophobic and sparsely charged unlike any of the other sequences used in analyses. Based on this unusual hydrophobic nature, this collagen-like protein may find its applications for procedures like guided tissue reconstruction in dentistry as also in hernia repair and topical wound dressings. In order to determine the potential of the collagen gene of Trichodesmium erythraeum for tissue engineering, further studies will be required that include experimentally measuring its thermal stability, enzymatic stability of the triglycine repeat region and the globular N and C termini and its ability to undergo fibrillogenesis using established methods.