Download or read book Design and Characterization of Peptide-based Biomaterials written by Sivakumar Ramachandran and published by . This book was released on 2007 with total page 94 pages. Available in PDF, EPUB and Kindle. Book excerpt: The main objective of this dissertation is to lay out the design principles involved in assembling stimuli-sensitive, peptide-based biomaterials that has potential for various biomedical applications like tissue engineering and drug delivery. Supramolecular systems, which enable one to assemble novel materials from molecular level, have fascinated researchers in many disciplines. Inspired by such systems, a set of mutually complementary, self-repulsive oligopeptide modules (with alternating polar-apolar amino acid sequence) were designed to gain better control and wide range of tunability over the assembling process. These peptide modules (at 0.25 wt% in aqueous buffer) assembled into a hydrogel network with change in pH/ionic strength (self-assembly) and upon mixing the two mutually-complementary peptide modules (co-assembly). Mixing induced hydrogels are particularly attractive as they can be easily assembled by simple mixing of peptide solutions prior to application. Another advantage of mixing-induced gelation is that it preserves the pH and ionic strength of the original peptide solutions. Circular dichroism spectroscopy of individual decapeptide solutions revealed their random coil conformation. Transmission electron microscopy images showed the nanofibrillar network structure of the hydrogel. Dynamic rheological characterization revealed its high elasticity and shear-thinning nature. Furthermore, the co-assembled hydrogel was capable of rapid recoveries from repeated shear-induced breakdowns, a property desirable for designing injectable biomaterials. A systematic variation of the neutral amino acids in the sequence revealed some of the design principles for this class of biomaterials. First, viscoelastic properties of the hydrogels can be tuned through adjusting the hydrophobicity of the neutral amino acids. Second, the beta-sheet propensity of the neutral amino acid residue in the peptides is critical for hydrogelation. The compatibility of these hydrogels with entrapped biomolecules (molecular biocompatibility) was confirmed using high-resolution, 1H-15N heteronuclear NMR spectroscopy. Sticky-ends in the peptide fibers did not provide any advantages over blunt-ends in terms of biomaterial property, suggesting that peptides might be aligned perpendicular to the fiber axis. Once the design principles of these peptide-based biomaterials are laid out, the next step would be to incorporate biological functionalities like cell-adhesive motifs and enzyme recognition sequences at strategic positions of these biomaterials for specific tissue engineering or drug delivery applications.