Abstract
Small-angle X-ray scattering (SAXS) was used to monitor peptide hydrogelation with and without the MRI contrast agent gadolinium chelate (Gd(III)-chelate). The gelators are a pair of decapeptides that are self-repulsive but mutually attractive. Gd(III)-chelate was either free or covalently bound to one of the decapeptides. Free and conjugated Gd(III)-chelate have the opposite effects on peptide gelation: free Gd(III)-chelate slows down gelation while having little effect on the cross-sectional area of peptide fibers; covalently conjugated Gd(III)-chelate speeds up gelation and results in peptide fibers with significantly greater cross-sectional area. After 24 h of gelation, the cross-sectional areas of hydrogels with no Gd(III)-chelate, with free Gd(III)-chelate and with conjugated Gd(III) chelate are 3700, 3800, and 6300 Å(2), respectively. Free Gd(III)-chelate is not incorporated into peptide fibers and remains in solution with little effect on MRI intensity upon gelation. In contrast, covalently conjugated Gd(III)-chelate is not only incorporated into peptide fibers, but further aggregates toward the center of the peptide fibers. In conclusion, to visualize hydrogelation using (1)H MRI, it is necessary to conjugate Gd(III)-chelate to the material covalently and use T(2)-weighted imaging.