Diffusivity of 125I-labelled macromolecules through collagen: mechanism of diffusion and effect of adsorption.
Diffusion of angiotensin II, albumin and aldolase was studied through collagen membranes with swelling ratios between 4 and 15. The diffusion coefficient was measured from the time-lag for the onset of steady-state flux through the membrane. Binding of macromolecules to collagen was evaluated from the results of sorption studies conducted as a function of macromolecular concentration. Results presented indicate that the diffusion of macromolecules through collagen membrane is slowed by electrostatic and hydrogen bonding between individual macromolecular chains and collagen. The extent of adsorption is increased as the molecular weight of the diffusant increases. Diffusion of water soluble macromolecules through collagen occurs rapidly, suggesting that diffusion occurs through water filled channels as opposed to between collagen molecules. The results of these studies are useful in understanding diffusion through connective tissues and in the design of drug delivery systems based on collagen.
D000327:Adsorption; D000418:Albumins; D000804:Angiotensin II; D000818:Animals; D001672:Biocompatible Materials; D003094:Collagen; D004058:Diffusion; D004563:Electrochemistry; D005634:Fructose-Bisphosphate Aldolase; D006860:Hydrogen Bonding; D066298:In Vitro Techniques; D007457:Iodine Radioisotopes; D007700:Kinetics; D010539:Permeability; D013816:Thermodynamics
D000418:Albumins; D001672:Biocompatible Materials; D007457:Iodine Radioisotopes; D000804:Angiotensin II; D003094:Collagen; D005634:Fructose-Bisphosphate Aldolase