Chemical synthesis of cross-linked poly(KGGVG), an elastin-like biopolymer.
Previous studies afforded on peptides and polypeptides containing repetitive sequences of elastin have largely demonstrated that their molecular and supramolecular properties are fully representative of those of tropoelastin, the soluble, linear precursor of elastin itself. In the attempt to synthesize cross-linked elastin-mimetic polypeptides, the repeating sequence VGGVG (V: valine; G: glycine), typical of elastin, was modified to incorporate lysine residues, yielding the polymer poly(KGGVG) (K: lysine). This imparts primary amine functionality susceptible to cross-linking reaction with appropriate bifunctional cross-linking reagents. We report herein the chemical synthesis and cross-linking of poly(KGGVG) with glutaraldehyde (GTA) and with disuccinimidyl glutarate (DSG). In both cases, the characterization of the polymers, both linear and cross-linked, has been carried out by CD spectroscopy and transmission electron microscopy measurements. The obtained results, although not conclusive, demonstrate that poly(KGGVG), both linear and cross-linked, may be considered very similar to tropoelastin and mature elastin, as concerns its molecular and supramolecular properties.
Martino
M
M
Department of Chemistry, University of Basilicata, Via N. Sauro 85, 85100 Potenza, Italy.
Tamburro
A M
AM
D000818:Animals; D001704:Biopolymers / Q000737:chemistry; D002942:Circular Dichroism; D003432:Cross-Linking Reagents; D004549:Elastin / Q000737:chemistry*; D006801:Humans; D008854:Microscopy, Electron; D018716:Molecular Mimicry; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry
D001704:Biopolymers; D003432:Cross-Linking Reagents; D010455:Peptides; C433724:poly(KGGVG); D004549:Elastin