Effects of Triton X-100 and Acyclovir on Human Serum Albumin Structure

The effects of acyclovir and Triton X-100 on the behavior of human serum albumin (HSA) in a acyclovir/HSA/H₂O system were studied by UV spectroscopy, fluorescence spectroscopy and polarization, conductivity, zeta potential, and circular dichroism. Both acyclovir and Triton X-100 affect the structure and behavior of HSA. The intrinsic fluorescence intensity, net charge of HSA and the conductivity of the system increase initially with increased acyclovir concentration, and the zeta potential of HSA decreases initially. The effects of Triton X-100 are similar to those of acyclovir except for the non-radiant energy transfer in the quenching process of Triton X-100 to HSA. The associating site of HSA with acyclovir is the same as that of HSA with Triton X-100.

Tianqing LiuEmail: