Abstract
Abstract Because proteins are polyampholytes, they can interact with poly-electrolytes, mainly through an electrostatic force. In this report we discuss the interaction of serum albumin, which is a major component of serum proteins, with synthetic polyelectrolytes using fluorescent measurement. Polycations interact with anionic amino acids in a relatively random fashion only above the isoelectric point of albumin. On the other hand, polyanions interact selectively with a specific site of albumin, the drug binding site II in which basic amino acids are localized.
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