| Summary: | 碩士 === 國立中央大學 === 化學工程與材料工程研究所 === 99 === In the past few decades, with the widely application of the peptide drug in medical treatment, the peptide synthesis and purification play important roles. The technology development of liquid-phase and solid-phase synthesis becomes mature state. However, there exists a problem that the purification yield decreases with the length of peptide chain or conformation effect. Therefore, we propose a new idea to improve the yield. First, use the solid-phase synthesis method to obtain part of the long-chain peptide. And after purifying these fragments, operate the ligation step in liquid phase. In order to find the common solvents for these peptides in the ligation step, we utilize the solubility parameter theory that widely used in polymer-solvent selection to study the hydrophobic and protected amino acids. We use the reverse-phase chromatography to investigate the solubility parameters of the designed 21 model peptides (Fmoc-Gly-Phe-X-Phe-Gly, -X- is replaced by 20 different amino acids), and then do the calculation to obtain the solubility parameters of hydrophobic and protected amino acids. In addition to comparing the results with Hoy software calculated data, the correlation of the experimental partition energy and hydrophobicity from the literature is also to be study. Finally, we take a peptide composed of protected amino acids to estimate its solubility parameters, find the suitable solvents and predict the retention behavior successfully. The result shows that apply the solubility parameter theory in RP-HPLC to study the hydrophobic and protected amino acids can not only do the help in peptide-solvent selection but also prediction the elution conditions.
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