Authors:

Jasmine McKinnie

Date Created:

Not specified

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About Paper:

Sialic acids, such as N-Acetylneuraminic acid (Neu5Ac), are widespread nine-carbon sugars typically found at the terminal positions of human glycoconjugates. These molecules play essential roles in host-pathogen interactions, aiding pathogenic bacteria in immune evasion through molecular mimicry. Many bacteria acquire Neu5Ac from host tissues and import it using tripartite ATP-independent periplasmic (TRAP) transporters, which consist of a periplasmic binding protein alongside membrane-spanning components. This study explored protein purification strategies for an engineered F3 nanobody designed to target a Neu5Ac-binding periplasmic protein. A key focus was optimizing buffer conditions to maximize nanobody yield and purity, specifically comparing phosphate-buffered saline (PBS) at pH 8.0 to the standard pH 7.4. Our results indicated that raising the buffer pH led to improved purification outcomes. Keywords: [no keywords provided]

Source:

Purdue University / 2025

Topics:

No topics listed

Co-authors:

Jasmine McKinnie