Abstract
Synthesis of hydrophobic peptides remains difficult due to internal aggregation of constituent amino acids via β-sheet formation, and also due to the association between the protected chains with the synthetic-support matrix. There are two types of amino acids: hydrophilic and hydrophobic. Each amino acid is chemically different, so the coupling efficiency of hydrophobic and hydrophilic amino acids also differs from each other. If large numbers of hydrophobic amino acids are present in a peptide sequence despite these difficult to synthesis. Here we developed a novel PS-TPGDD resin as a solid support for the synthesis of hydrophobic peptide, which is still a challenge to peptide chemistry. The most essential biologically active hydrophobic peptide T-1-Conotoxin (IINWCCLIFYQCC) was successfully synthesized and some synthetic modification was performed using the Fmoc SPPS method.
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