Albumin has consistently demonstrated its potential for enhancing the delivery of drugs and polymer-drug conjugates, binding via supramolecular forces within its multiple binding sites. Herein, we introduce saturation transfer difference (STD-NMR) as a method to identify the interactions between a polymer library and bovine serum albumin (BSA). With STD-NMR, the binding ability of polymers can be quickly screened by focusing on their individual structural features, making this technique more suitable for high throughput screening in comparison to traditional fluorescence studies.