Blood–pool or intravascular contrast agents (BPCAs) for magnetic resonance imaging (MRI) are specifically designed to stay in the vascular system for a prolonged time. Human serum albumin (HSA), produced by the liver, is the most abundant protein found in blood. Employing current knowledge about which molecules are capable of binding to HSA, synthesis was directed in order to create an iron(III) complex able to bind to this protein and make an effective blood–pool contrast agent. Two ligands were synthesized based upon the molecule maltol: one with beta-alanine inserted into the maltol ring and another with ethylene diamine (or diethylamine) inserted into the ring. Beta-alanine contains a carboxyl group, while ethylene diamine contains an amine group. Each ligand was then used to create a complex with iron(III). Using Brüker minispec, the T1 spin-lattice relaxation rate was measured for each sample by plotting 1/T1 verses concentration (the slope is the relaxivity, R1) in both water and HSA solutions. The steeper the slope was interpreted as a more effective contrast agent, and the comparison between the contrast agent in water and the protein solution indicates if any significant binding takes place. The T1 values for each iron compound were measured at concentrations of 2.5mM, 5.0mM, 7.5mM, and 10.0mM. The iron(III) complex of beta-alaninemaltol derivative had a significantly higher relaxivity in HSA solution than in water, while the relaxivity decreased for the diethylaminemaltol derivative. Thus compounds with a carboxyl group are more suitable for BPCA contrast agents.