A novel and efficient approach for the amidation of C-terminal peptides

Arabanian, Armin; Mohammadnejad, M.; Balalaie, Saeed

doi:10.1007/bf03246077

Cited by 16 publications

(5 citation statements)

References 13 publications

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“…The five FXPRL neuropeptides released from the Marvi-DH-PBAN precursor were cleaved at six potential endoproteolytic cleavage sites that, except for the K-K site, share a conserved sequence of G-(K/R)-R ( Figure 1 ). Whereas the basic arginine residue is served as a canonical signal preceding the cleavage sites [43] , the presence of the glycine residue further indicated amidation of the C -terminus of neuropeptides in Marvi-DH-PBAN, which is pivotal for the biological activity of peptide hormones [44] . The cleavage motif of basic K-K residues has been reported to occur less frequently in neuropeptide precursors; however, it was observed being cleaved in 64% of its occurrence in Apis mellifera and Drosophila melanogaster [41] ; thus it was not surprising to find it present in the Marvi-DH-PBAN.…”

Section: Discussionmentioning

confidence: 99%

Identification and Expression Analysis of Diapause Hormone and Pheromone Biosynthesis Activating Neuropeptide (DH-PBAN) in the Legume Pod Borer, Maruca vitrata Fabricius

Chang

Srinivasan

2014

PLoS ONE

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Neuropeptides play essential roles in a variety of physiological responses that contribute to the development and reproduction of insects. Both the diapause hormone (DH) and pheromone biosynthesis activating neuropeptide (PBAN) belong to the PBAN/pyrokinin neuropeptide family, which has a conserved pentapeptide motif FXPRL at the C-terminus. We identified the full-length cDNA encoding DH-PBAN in Maruca vitrata, a major lepidopteran pest of leguminous crops. The open reading frame of Marvi-DH-PBAN is 591 bp in length, encoding 197 amino acids, from which five putative neuropeptides [DH, PBAN, α-subesophageal ganglion neuropeptide (SGNP), β-SGNP and γ-SGNP] are derived. Marvi-DH-PBAN was highly similar (83%) to DH-PBAN of Omphisa fuscidentalis (Lepidoptera: Crambidae), but possesses a unique C-terminal FNPRL motif, where asparagine has replaced a serine residue present in other lepidopteran PBAN peptides. The genomic DNA sequence of Marvi-DH-PBAN is 6,231 bp in size and is composed of six exons. Phylogenetic analysis has revealed that the Marvi-DH-PBAN protein sequence is closest to its homolog in Crambidae, but distant from Diptera, Coleoptera and Hymenoptera DH-PBAN, which agrees with the current taxonomy. DH-PBAN transcripts were present in the head and thoracic complex, but absent in the abdomen of M. vitrata. Real-time quantitative PCR assays have demonstrated a relatively higher expression of Marvi-DH-PBAN mRNA in the latter half of the pupal stages and in adults. These findings represent a significant step forward in our understanding of the DH-PBAN gene architecture and phylogeny, and raise the possibility of using Marvi-DH-PBAN to manage M. vitrata populations through molecular techniques.

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Section: Discussionmentioning

confidence: 99%

Identification and Expression Analysis of Diapause Hormone and Pheromone Biosynthesis Activating Neuropeptide (DH-PBAN) in the Legume Pod Borer, Maruca vitrata Fabricius

Chang

Srinivasan

2014

PLoS ONE

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“…The cleavage of the peptide analog from the resin was done using TFA 1%. The C‐terminus amidation of the peptide sequence was done using ammonium chloride and TBTU in the presence of N ‐methylmorpholine to give peptide 12 in solution phase . Final deprotection was done using TFA 95% and reagent K.…”

Section: Resultsmentioning

confidence: 96%

Design, Synthesis and Biological Evaluation of Triptorelin Analogs Containing Tetrazole Moiety

et al. 2020

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The design and synthesis of novel bioisosteric analogues of triptorelin acetate containing tetrazole moiety at C‐ or N‐terminus of the peptides is described. Tetrazole acetic acid was synthesized through the reaction of an alkyl cyanoacetate and sodium azide, after that, it was coupled to the N‐terminus of triptorelin instead of pyroglutamic acid. In another approach, tetrazole acetohydrazide was prepared and conjugated to the C‐terminus of triptorelin instead of the amide bond. The synthesized peptides containing tetrazole moiety at the C‐ or N‐terminus of the peptide sequence are peptidomimetics of triptorelin acetate. The docking results of the designed derivatives showed the same interaction of triptorelin with the receptor but with a higher score.The peptide that has tetrazole moiety in its C‐terminus, restricted the testosterone level during four weeks of in vivo study and led to keep testosterone at a moderate level during the first week compared to control.

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“… For details of the synthesis of [Met5]enkephalin amide, ethylamide and semicarbazide, see Arabanian et al . MALDI MS data show the molecular ion peaks (M + 1) + and 1 H, and 13 C‐NMR confirmed the structure.…”

Section: Methodsmentioning

confidence: 96%

“…Considering the key role of C‐terminal moiety of enkephalins on biological activity, in the present study, the antinociceptive effects of a newly synthesized enkephalin derivative, H‐Tyr‐Gly‐Gly‐Phe‐(Met)‐NH‐CO‐NH 2 , was compared with ME, MEA and ME‐ethylamide.…”

Section: Introductionmentioning

confidence: 99%

Antinociceptive effect of [Met5]enkephalin semicarbazide is not affected by dipeptidyl carboxypeptidase‐I

Rezaee

Arabanian

Balalaie

et al. 2011

Journal of Peptide Science

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Dipeptidyl carboxypeptidase-I is an enzyme involved in the biological degradation of enkephalins. It has been suggested that C-terminal amidation of enkephalins enhances their resistance to dipeptidyl carboxypeptidase-I-mediated biodegradation. In this study, a novel [Met5]enkephalin amide (MEA) analogue [Met5]enkephalin (ME)-semicarbazide synthesized by another laboratory in our group was assessed for its antinociceptive effects compared with ME-ethylamide, MEA and ME, using tail flick test. To protect the administered drugs from biodegradation, rats were pretreated with peptidase inhibitors including amastatin, phosphoramidon and captopril. Then captopril (dipeptidyl carboxypeptidase-I inhibitor) was deleted from the peptidase inhibitors' combination for evaluating in vivo resistance of the synthetic drugs to dipeptidyl carboxypeptidase-I. According to the results, ME-semicarbazide and MEA were resistant enough to dipeptidyl carboxypeptidase-I to exert their strong antinociception following intrathecal administration even in the absence of captopril, whereas the antinociceptive effects produced by ME-ethylamide (10 nmol) were abolished in rats not pretreated with captopril, indicating that significant amounts of the ME-ethylamide were degraded by dipeptidyl carboxypeptidase-I. Replacement of the amide moiety of MEA with semicarbazide provides a new ME derivative, with high analgesic effects as well as more resistance to dipeptidyl carboxypeptidase-I-mediated biodegradation.

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A novel and efficient approach for the amidation of C-terminal peptides

Cited by 16 publications

References 13 publications

Identification and Expression Analysis of Diapause Hormone and Pheromone Biosynthesis Activating Neuropeptide (DH-PBAN) in the Legume Pod Borer, Maruca vitrata Fabricius

Identification and Expression Analysis of Diapause Hormone and Pheromone Biosynthesis Activating Neuropeptide (DH-PBAN) in the Legume Pod Borer, Maruca vitrata Fabricius

Design, Synthesis and Biological Evaluation of Triptorelin Analogs Containing Tetrazole Moiety

Antinociceptive effect of [Met5]enkephalin semicarbazide is not affected by dipeptidyl carboxypeptidase‐I

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