Polypeptide-based acidic proteinoid containing L-glutamic acid and L-aspartic acid in excess and five other neutral and basic amino acids in minor proportions have been synthesized and found that it forms organized aggregates in an aqueous solution. The proteinoid aggregate has been characterized using C-13-NMR, IR, and fluorescence spectroscopic techniques. The c.m.c. of the proteinoid has been determined by conductometric and pH metric methods. The aggregation studies were carried out at different temperatures and varying ionic strengths of the medium. The phase transition of the proteinoid aggregate has been determined using the fluorescence absorbance method. The aggregation behavior is shown to be dependent on the pH of the solution. This was also supported by conductivity measurements. Using methylene blue as a model drug, the drug delivery property of the proteinoid micelles were studied in acidic (pH 4.5) and neutral (pH 7.4) mediums. Using biphasic model thermochemical parameters, Delta G, Delta H, Delta S, and Delta C-p have been evaluated.