Abstract
The nonspecific binding of peptides to material surfaces is a well-known phenomenon that makes measurement of these substances challenging. Peptide adsorption can be reduced with suitable materials or additives, but the complex nature of biomolecules makes it challenging to find an universal sample preparation method. This study focused on investigating the surface adsorption behavior of motilin to enhance the sensitivity and precision of analytical methods. A simple and specific HPLC method was developed for the quantification of motilin. Using this chromatographic method, it was discovered that motilin binds to both polypropylene and glass surfaces at high levels, with recovery rates of 32 and 24%, respectively. To mitigate this, the effect of protein (bovine serum albumin), salt (sodium chloride), and surfactant (Tween 80) on surface adsorption was investigated. Although all additives reduced adsorption, only Tween 80 achieved nearly 100% recovery with consistent results (RSD ≤2%). Consequently, the sample preparation procedure developed using Tween 80 was integrated into the HPLC method, and the method was validated according to the International Conference on Harmonization guideline [ICH Q2(R1)]. This method is expected to have potential applications in analytical chemistry, drug development, biotechnology, and the pharmaceutical industry for providing accurate and dependable peptide measurements.
Published Version
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