Saturation Transfer Difference NMR Spectroscopy for the Elucidation of Supramolecular Albumin–Polymer Interactions

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 p...

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Bibliographic Details
Published inACS macro letters Vol. 10; no. 7; pp. 819 - 824
Main Authors Xu, You D, Lai, Rebecca Y, Procházková, Eliška, Stenzel, Martina H
Format Journal Article
LanguageEnglish
Published United States American Chemical Society 20.07.2021
Subjects
Binding Sites
Magnetic Resonance Spectroscopy - methods
Polymers - metabolism
Protein Binding
Serum Albumin, Bovine - chemistry
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Summary: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.
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ISSN:2161-1653
2161-1653
DOI:10.1021/acsmacrolett.1c00270