---

Introduction: Given the importance of human serum albumin, evaluation of the protein is invaluable. One of the characteristics of the protein is to create ligand bindings. The trait was assessed by application of the surfactant, sodium dodecyl sulfate (SDS), as a ligand under normal and pathologic temperatures and normal and diabetic concentration of glucose. Material & Methods: UV spectroscopy was the method used in this experiment. Human Serum albumin was evaluated in the presence of different concentrations of glucose and the following conditions: SDS at the conce-ntrations, 2, 1.5, 1, and 0.5mM as indices for ligand binding assay, and normal and fever temperatures. Findings: The high temperature 42°C and different concentrations of glucose created structural changes in albumin. This effect was more significant at 400 mg/dl conce-ntration of glucose. Discussion & Conclusion: Human Serum Albumin structure was highly affected by increment of temperate which was more evident in diabetic condition.