Preparation of a gelatin-binding conjugate containing gold thiomalate.
Plasma fibronectin has a range of binding sites, for ligands, including denaturated collagen (gelatin). It has been proposed that this activity may be used for nonimmune drug targeting to sites in the extra-cellular matrix such as the targeting of gold thiomalate to rheumatoid joints. In the present study, a novel conjugate has been developed, consisting of the gold thiomalate bound at high density to the gelatin-binding domain of fibronectin, through a polylysine carrier. Isolation and cross-linking of suitable fragments of fibronectin (relative molecular weights 65 and 52 kDa) to polylysine is followed by conjugation to gold thiomalate on a solid phase, gelatin-agarose affinity absorbent. Although gold thiomalate has the ability to inactivate, the protein-gold conjugate produced by this technique retained its gelatin-binding activity.[1]References
- Preparation of a gelatin-binding conjugate containing gold thiomalate. Brown, R.A., More, J., Ejim, O.S. Arzneimittel-Forschung. (1993) [Pubmed]
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