Direct evidence for the function of crustacean insulin-like androgenic gland factor (IAG): Total chemical synthesis of IAG

Journal of Peptide Science

Mukainakano

Kogure

et al. 2018

Self Cite

Among the insulin‐family peptides, two additional cysteine residues other than six conserved cysteines are sometimes found in invertebrate insulin‐like peptides (ILPs), although the synthetic method for such four disulfide ILPs has not yet been well established. In this study, we synthesized a crustacean insulin‐like androgenic gland factor with four disulfides by the regioselective disulfide bond formation reactions using four orthogonal Cys‐protecting groups. Its disulfide isomer could be also synthesized by the same method, indicating that the synthetic strategy developed in this study might be useful for the synthesis of other four disulfide ILPs.

Section: Resultssupporting

confidence: 89%

“…In our previous study, we used DPDS in trifluoromethanesulfonic acid (TfOH)/TFA solution for deprotecting MeOBn group . However, this reaction conditions were quite similar to those for the removal of Bu t group reported previously .…”

Section: Resultsmentioning

confidence: 94%

Chemical synthesis of the crustacean insulin‐like peptide with four disulfide bonds

Journal of Peptide Science

Mukainakano

Kogure

et al. 2018

Self Cite

“…The helix contents of peptides 12 (44.5%) and 13 (35.5%) are also almost comparable with the glycosylated peptides, indicating that the N ‐linked glycan moiety did not affect the peptide conformation in both disulfide isomers. It has been reported that the glycosylation affected the peptide conformation of M japonicus IAG . Since the glycosylation is essential for conferring the hormonal activity, it is presumed that the conformation significant for the biological activity is stabilized by the glycosylation in M japonicus IAG.…”

Section: Resultsmentioning

confidence: 99%

“…It was shown that the glycosylation affected the peptide conformation of M japonicus IAG . Furthermore, the N ‐glycosylation site is conserved among Penaeidea crustacean IAGs .…”

Section: Introductionmentioning

confidence: 99%

Chemical synthesis of N‐glycosylated insulin‐like androgenic gland factor from the freshwater prawn Macrobrachium rosenbergii

Journal of Peptide Science

Nagasawa

2019

Self Cite

Crustacean insulin‐like androgenic gland factor (IAG) of Macrobrachium rosenbergii, a heterodimeric peptide having both four disulfide bonds and an N‐linked glycan, was synthesized by the combination of solid‐phase peptide synthesis and the regioselective disulfide formation reactions. The disulfide isomer of IAG could also be synthesized by the same manner. The conformational analysis of these peptides by circular dichroism (CD) spectral measurement indicated that the disulfide bond arrangement affected the peptide conformation in IAG. On the other hand, the N‐linked glycan attached at A chain showed no effect on CD spectra of IAG. This is the first report for the chemical synthesis of insulin‐like heterodimeric glycopeptide having three interchain disulfides, and the synthetic strategy shown here might be useful for the synthesis of other glycosylated four‐disulfide insulin‐like peptides.

“…As expected, this peak material gave the molecular ion peak at m / z 4202.5 in the mass spectral analysis, and this value coincided well with the calculated number of the desired glycopeptide 5 , indicating that the protecting groups on the carbohydrate moiety could be removed by the TFA cocktail treatment. The isolated yield of glycopeptide 5 after the RP‐HPLC purification was 15%, and this value was higher than that in the case using Bn‐protected Asn(GlcNAc) derivative (11% yield ).…”

Section: Methodsmentioning

confidence: 71%

Facile preparation of the N -acetyl-glucosaminylated asparagine derivative with TFA-sensitive protecting groups useful for solid-phase glycopeptide synthesis

2015

J. Pept. Sci.

Self Cite

In this study, a novel N-acetyl-glucosaminylated asparagine derivative was developed. This derivative carried TFA-sensitive protecting groups and was derived from commercially available compounds only in three steps. It was applicable to the ordinary 9-fluorenylmethoxycarbonyl (Fmoc)-based solid-phase peptide synthesis (SPPS) method, and the protecting groups on the carbohydrate moiety could be removed by a single step of TFA cocktail treatment generally used for the final deprotection step in Fmoc-SPPS.