title: Synthesis of biologically important neutral amylo-β peptide by using improved Fmoc solid-phase peptide synthetic strategy.
abstract: 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. Graphical abstractᅟ.
authors: Research and Development Centre, Bharathiar University, Coimbatore, 641046 India.
authors: R
authors: R
authors: Selvam
authors: R&D Centre, JNTU, Hyderabad, 500085 India.
authors: E
authors: E
authors: Sudha
authors: Research and Development Centre, Bharathiar University, Coimbatore, 641046 India.
authors: P R
authors: PR
authors: Rajkumar
authors: Research and PG Department of Chemistry, Sri Vyasa NSS College, Thrissur, Kerala 680623 India.
authors: K P
authors: KP
authors: Subashchandran
keywords: Amylo-β peptide; Fmoc SPPS; HoBt and DIC; Polymer support