CHARACTERIZATION OF THE ADSORPTION PROCESS ANALOGOUS PEPTIDES ON ALUMINA GEL

peptide antigen adsorption on aluminum hydroxide gel must be characterized when formulating vaccines. in this work a peptide belonging to the amino-terminal region of plasmodium falciparum merozoite surface protein and its analogues have been characterized. the adsorption of 17 analogues on aluminum hydroxide which had greater than 10 mmol/l solubility was quantified at 298 k. adsorption capacity and affinity constant parameters were calculated by applying the langmuir's adsorption model. the results have been presented in three groups according to adsorption isotherm trajectory. the first group consists of analogues where the first organization of peptide molecules was presented at low concentrations, followed by a rapid increase in adsorption to high concentrations. the second group consists of analogues having an adsorption pattern showing the formation of a first layer at low peptide concentrations and a second layer at greater concentrations. the third group contains analogues whose adsorption involved the formation of two simple layers, this being differentiated from the second group in that after the second layer had been completed, the amount adsorbed grew notably with increased concentration. the results revealed a more complex pattern that monolayer or bilayer formation. this work constitutes the first approach towards establishing an adsorbed layer structure model using a peptide system.