Journal of Chemical Biology | |
Synthesis of biologically important neutral amylo-β peptide by using improved Fmoc solid-phase peptide synthetic strategy | |
K. P. Subashchandran1  R. Selvam1  E. Sudha1  P. R. Rajkumar1  | |
[1] Research and Development Centre, Bharathiar University, Coimbatore, 641046 India | |
关键词: Polymer support; Amylo-β peptide; Fmoc SPPS; HoBt and DIC; | |
DOI : 10.1007/s12154-015-0128-2 | |
学科分类:分子生物学,细胞生物学和基因 | |
来源: Springer | |
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【 摘 要 】
The 10 amino acid sequence of the biologically important neutral amylo-β peptide has equally hydrophilic and hydrophobic properties, which reduces the coupling efficiency during its synthesis and reduces the final yield of the peptide, and is therefore classified as a “difficult peptide sequence.” The method presented here minimizes the synthetic problems by the introduction of improved Fmoc chemistry and effective hydroxybenzotriazole (HoBt), diisopropylcarbodiimide (DIC)-coupling and activation strategies. In addition, we developed a PS-TPGD resin as a solid support for the synthesis of specific neutral peptides, which is still a challenge to peptide chemistry. The most essential biologically active neutral amylo-β peptide (KVKRIILARS) was successfully synthesized, and some synthetic modification was performed using the Fmoc solid-phase peptide synthesis (SPPS) method for purity and yield improvement.
【 授权许可】
Unknown
【 预 览 】
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