백지인 (충남대학교)

윤소희 (한국표준과학연구원)

백지인 (충남대학교)

송지영 (UST)

윤소희 (한국표준과학연구원)

 Albumin is the most abundant protein in serum and plays a crucial role in drug delivery and diagnostic platforms due to its excellent biocompatibility, binding affinity, and structural stability. Despite its broad biomedical applications, accurate quantification of albumin remains experimentally challenging. In particular, Matrix-Assisted Laser Desorption/Ionization Time-of-Flight (MALDI-TOF) mass spectrometry, while highly effective for qualitative analysis, often suffers from limited reproducibility and precision in quantitative applications due to variables such as matrix selection, sample distribution, and laser parameters.This study aimed to optimize MALDI-TOF MS conditions for albumin quantification by evaluating the effects of matrix type, sample plate, and laser beam irradiation mode. Among the matrices tested—α-Cyano-4-hydroxycinnamic acid (CHCA), 2,5-Dihydroxybenzoic acid (DHB), Sinapinic acid (SA), and 2,5-Dihydroxyacetophenone (DHAP)—DHAP provided the highest ionization efficiency and signal intensity.The laser mode that splits the beam into five parts at a single spot (M5 Flat) produced the most stable and intense spectra, allowing a reduction in the number of laser shots per spectrum from 15,000 to 2,000 without compromising spectral quality.Comparison of sample plates revealed that AnchorChip plates enhanced qualitative sensitivity by concentrating the sample, whereas polished steel plates ensured higher reproducibility in quantitative measurements due to more uniform sample distribution. In summary, the combination of DHAP, polished steel plates, and M5 Flat laser mode was identified as the optimal condition for reproducible albumin quantification using MALDI-TOF MS. These findings provide a valuable strategy for improving the reliability of protein quantification in clinical diagnostics and nanodrug development.