What is true about the selectivity of protein binding for drugs?

The selectivity of protein binding for drugs involves the ability of drugs to compete for binding sites on plasma proteins, such as albumin and alpha-1 acid glycoprotein. Many drugs can exhibit similar chemical properties, which may lead them to compete for these limited binding sites. This competition can influence the distribution and effectiveness of the drugs because only the unbound fraction is pharmacologically active.

While it is true that certain drugs may have predilection towards specific binding sites, the concept of competition among similar drugs highlights the dynamic nature of protein binding. When multiple drugs are present, the binding of one drug can displace another, leading to changes in the levels of free (active) drug in circulation.

The notion that only fats can bind with proteins is incorrect, as many diverse molecules, including both hydrophilic and lipophilic drugs, can bind to proteins. The assertion pertaining to a preference for basic drugs over acidic ones also lacks support, as various drugs across both categories can bind effectively depending on their specific characteristics and the nature of the proteins. The selectivity in protein binding is not merely a straightforward preference, but rather a complex interplay of molecular interactions.