Buffer Influence on the Amino Acid Silica Interaction.
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ABSTRACT: Protein-surface interactions are exploited in various processes in life sciences and biotechnology. Many of such processes are performed in presence of a buffer system, which is generally believed to have an influence on the protein-surface interaction but is rarely investigated systematically. Combining experimental and theoretical methodologies, we herein demonstrate the strong influence of the buffer type on protein-surface interactions. Using state of the art chromatographic experiments, we measure the interaction between individual amino acids and silica, as a reference to understand protein-surface interactions. Among all the 20 proteinogenic amino acids studied, we found that arginine (R) and lysine (K) bind most strongly to silica, a finding validated by free energy calculations. W
SUBMITTER: Bag S
PROVIDER: S-EPMC7702087 | biostudies-literature | 2020 Oct
REPOSITORIES: biostudies-literature
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