Novel protocol for the chemical synthesis of crustacean hyperglycemic hormone analogues--an efficient experimental tool for studying their functions
Autor: | Sándor Pongor, Sotir Zahariev, Corrado Guarnaccia, Vientsislav Zlatev, Antonella Campanella, Alessandro Mosco, Piero Giulio Giulianini |
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Přispěvatelé: | Mosco, Alessandro, Zlatev, Ventsislav, Guarnaccia, C., Pongor, S., Campanella, A., Zahariev, S., Giulianini, PIERO GIULIO |
Jazyk: | angličtina |
Rok vydání: | 2012 |
Předmět: |
Proteomics
Spectrometry Mass Electrospray Ionization Anatomy and Physiology Invertebrate Hormones Molecular Sequence Data lcsh:Medicine Nerve Tissue Proteins Endocrine System Marine Biology Peptide Astacoidea Biology Biochemistry Chemical synthesis Arthropod Proteins chemistry.chemical_compound Isomerism crustacean hyperglycemic hormone Peptide synthesis Animals Amino Acid Sequence lcsh:Science Peptide sequence Chromatography High Pressure Liquid Solid-Phase Synthesis Techniques cHH chemistry.chemical_classification Chromatography Reverse-Phase Multidisciplinary Endocrine Physiology lcsh:R Proteins Biological activity Native chemical ligation Amino acid Glucose chemistry chemical synthesis Hyperglycemia Biological Assay lcsh:Q Invertebrate hormone Peptides Research Article |
Zdroj: | PLoS ONE, Vol 7, Iss 1, p e30052 (2012) PLoS ONE |
ISSN: | 1932-6203 |
Popis: | The crustacean Hyperglycemic Hormone (cHH) is present in many decapods in different isoforms, whose specific biological functions are still poorly understood. Here we report on the first chemical synthesis of three distinct isoforms of the cHH of Astacus leptodactylus carried out by solid phase peptide synthesis coupled to native chemical ligation. The synthetic 72 amino acid long peptide amides, containing L- or D-Phe3 and (Glp1, D-Phe3) were tested for their biological activity by means of homologous in vivo bioassays. The hyperglycemic activity of the D-isoforms was significantly higher than that of the L-isoform, while the presence of the N-terminal Glp residue had no influence on the peptide activity. The results show that the presence of D-Phe3 modifies the cHH functionality, contributing to the diversification of the hormone pool. |
Databáze: | OpenAIRE |
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