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Chemical synthesis of cross‐linked poly(KGGVG), an elastin‐like biopolymer
Author(s) -
Martino M.,
Tamburro A. M.
Publication year - 2001
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/1097-0282(200107)59:1<29::aid-bip1003>3.0.co;2-f
Subject(s) - elastin , tropoelastin , chemistry , glutaraldehyde , supramolecular chemistry , desmosine , lysine , biopolymer , polymer chemistry , polymer , amine gas treating , biochemistry , organic chemistry , molecule , amino acid , extracellular matrix , medicine , pathology
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. © 2001 John Wiley & Sons, Inc. Biopolymers 59: 29–37, 2001