Synthesis of biologically important neutral amylo-β peptide by using improved Fmoc solid-phase peptide synthetic strategy

Journal of Chemical Biology

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

【 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