Hyaluronan-Arginine Interactions-An Ultrasound and ITC Study

Abstract

High-resolution ultrasound spectroscopy and isothermal titration calorimetry were used to characterize interactions between hyaluronan and arginine oligomers. The molecular weight of arginine oligomer plays an important role in interactions with hyaluronan. Interactions were observable for arginine oligomers with eight monomer units and longer chains. The effect of the ionic strength and molecular weight of hyaluronan on interactions was tested. In an environment with increased ionic strength, the length of the arginine oligomer was crucial. Generally, sufficiently high ionic strength suppresses interactions between hyaluronan and arginine oligomers, which demonstrated interactions in water. From the point of view of the molecular weight of hyaluronan, the transition between the rod conformation and the random coil conformation appeared to be important.High-resolution ultrasound spectroscopy and isothermal titration calorimetry were used to characterize interactions between hyaluronan and arginine oligomers. The molecular weight of arginine oligomer plays an important role in interactions with hyaluronan. Interactions were observable for arginine oligomers with eight monomer units and longer chains. The effect of the ionic strength and molecular weight of hyaluronan on interactions was tested. In an environment with increased ionic strength, the length of the arginine oligomer was crucial. Generally, sufficiently high ionic strength suppresses interactions between hyaluronan and arginine oligomers, which demonstrated interactions in water. From the point of view of the molecular weight of hyaluronan, the transition between the rod conformation and the random coil conformation appeared to be important.