Preparation of well-defined poly(ether-ester) macromers: photogelation and biodegradability.

Two series of poly(ether-ester)-based bis-functional macromers terminated with acrylate groups and a well-defined number of ester bonds were synthesized. One series had a chain of 1, 3 or 5 ester bonds at both ends of the central poly(ethylene glycol) block (molecular weight, about 1000), while the other had an alternating structure of oligo(ethylene glycol) each of them linked to two ester bonds, in which 6 or 10 ester bonds were incorporated equally in the macromer molecules and the total molecular weight was adjusted by about 1000. Irradiation of all poly(ether-ester) macromers mixed with camphorquinone resulted in the formation of gels. Gel yield increased and hydrophilic properties of the gels produced decreased with irradiation time. The elastic modulus of the gels decreased with the number of ester bonds. Upon incubation in a PBS solution (pH 8.04), all gels were gradually degraded with time. At 3 weeks of incubation, the degradation ratio increased linearly with the number of ester bonds per unit of molecular weight of the macromers. The order of in vivo degradation rates determined from weight loss was similar to that of the in vitro study. Thus, these poly(ether-ester) macromers may be useful for biodegradable biomaterials or tissue engineering scaffolds.

Study of wheat high molecular weight 1Dx5 subunit by (13)C and (1)H solid-state NMR. II. Roles of nonrepetitive terminal domains and length of repetitive domain.

This work follows a previous article that addressed the role of disulfide bonds in the behavior of the 1Dx5 subunit upon hydration. Here the roles of nonrepetitive terminal domains present and the length of the central repetitive domain in the hydration of 1Dx5 are investigated. This was achieved by comparing the hydration behavior of suitable model samples determined by (13)C- and (1)H-NMR: an alkylated 1Dx5 subunit (alk1Dx5), a recombinant 58-kDa peptide corresponding to the central repetitive domain of 1Dx5 (i.e., lacking the terminal domains), and two synthetic peptides (with 6 and 21 amino acid residues) based on the consensus repeat motifs of the central domain. The (13)C cross-polarization and magic angle spinning (MAS) experiments recorded as a function of hydration gave information about the protein or peptide fractions resisting plasticization. Conversely, (13)C single pulse excitation and (1)H-MAS gave information on the more plasticized segments. The results are consistent with the previous proposal of a hydrated network held by hydrogen-bonded glutamines and possibly hydrophobic interactions. The nonrepetitive terminal domains were found to induce water insolubility and a generally higher network hindrance. Shorter chain lengths were shown to increase plasticization and water solubility. However, at low water contents, the 21-mer peptide was characterized by higher hindrance in the megahertz and kilohertz frequency ranges compared to the longer peptide; and a tendency for a few hydrogen-bonded glutamines and hydrophobic residues to remain relatively hindered was still observed, as for the protein and large peptide. It is suggested that this ability is strongly dependent on the peptide primary structure.