Synthesis of Biologically Active Hydrophobic Peptide by Using Novel Polymer Support: Improved Fmoc Solid Phase Methodology

Autor:	K. P. Subashchandran, R. Selvam
Rok vydání:	2014
Předmět:	chemistry.chemical_classification Chemistry Bioengineering Biological activity Peptide Polymer Biochemistry Combinatorial chemistry Analytical Chemistry Amino acid Matrix (chemical analysis) Phase (matter) Drug Discovery Peptide chemistry Molecular Medicine Organic chemistry Peptide sequence
Zdroj:	International Journal of Peptide Research and Therapeutics. 21:91-97
ISSN:	1573-3904 1573-3149
DOI:	10.1007/s10989-014-9431-y
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::918f3cce65cb84927e12394ca461e29e https://doi.org/10.1007/s10989-014-9431-y Zobrazit plný text záznamu Full text from SpringerLink