Abstract
Hydrogels based on marine natural biopolymers have extensive possibilities for application in regenerative medicine, being best fit from safety and toxicity point of view, inexpensive and commercially available materials for 3D tissue scaffold development. In this study a peptide fraction from the temperate sea cucumber species Parastichopus tremulus has been characterized by de novo sequencing. ORAC antioxidant activity of 0,35 ± 0,05 TE/μg protein; IC50 of 22% and capacity to self-assemble into transparent hydrogel under physiological conditions have been experimentally determined. 926 MALDI-TOF peptide sequences were identified to belong to four protein types on basis of homology with Apostichopus japonicus and sea urchin proteins – major yolk protein, non-skeletal actin, collagen, and cluster BSL78-belonging. The surface hydrophobicity, gelation, and cytotoxicity of the P. tremulus peptides were studied and 13 peptide sequences from the collagen group were predicted in silico to have auto-assembly capacity.
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