Total solid-phase synthesis of porcine gut gastrin releasing peptide (GRP), a mammalian bombesin

Maerki, W.; Spiess, Joachim; Taché, Y.; Brown, Marvin R.; Rivier, Jean

doi:10.1021/ja00401a040

Cited by 78 publications

(26 citation statements)

References 9 publications

(21 reference statements)

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“…Peptides were synthesized by the solid-phase approach using protocols described elsewhere (11,12). The peptide content of the lyophilized samples was determined by amino acid analysis.…”

Section: Methodsmentioning

confidence: 99%

Structural homology of corticotropin-releasing factor, sauvagine, and urotensin I: circular dichroism and prediction studies.

Pallai¹,

Mabilia²,

Goodman³

et al. 1983

Proc. Natl. Acad. Sci. U.S.A.

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Three recently isolated peptides, whose sequences have been determined-the corticotropin (adrenocorticotropic hormone)-releasing factor of ovine origin, sauvagine, from the skin of the frog Phyllomedusa sauvagei, and urotensin I from the teleost fish, Catostomu commersoni-show high (>50%) sequence homology. CD spectra of the three peptides in trifluoroethanol indicate predominantly helical character for these peptides. Analysis of the secondary structures by the Chou-Fasman method predicts that the overall structural organization of the peptides is the same. All three possess a long internal helix, spanning about 25 residues, connected by a turn region to a COOHterminal structural element that is an a-helix in corticotropin-releasing factor and urotensin I and a fl-sheet in sauvagine. The values for helical content estimated from the prediction method agree reasonably well with those computed from the CD spectra. This agreement as well as the CD spectra of corticotropin-releasing factor fragment 5-33 support the specific assignments of helical regions derived from the Chou-Fasman analysis. The three peptides exhibit significantly less helical structure in water than in trifluoroethanol as indicated by CD spectra. Hydrophilicity profiles provided comparison of the three peptides in terms of their overall hydrophilicity and the location of the regions of maximal hydrophilicity. A unique distribution of hydrophilic and hydrophobic residues within the internal helices is revealed by helical wheel analysis. Patches of both types of residues are formed following a heptad (four/three) rule. Since the two patches are shifted by one residue relative to one another, together they occupy only one face of the helical surface, a feature distinct from other amphiphilic structures.The presence of a corticotropin (adrenocorticotropic hormone)-releasing factor (CRF) in the hypothalamus was established more than 25 years ago (1-3). Its characterization from ovine hypothalami was achieved only very recently (4, 5). Synthetic CRF has been shown to release ACTH and 1-endorphin both in vitro and in vivo and to cause hypotensive and behavioral effects in rats (4, 6). Sauvagine, a 40-amino acid peptide, highly homologous with CRF, was isolated from the skin of the frog Phylonmedusa sauvagei (7) and displays, among other activities, a number of CRF-like effects, such as release of ACTH and , 1 endorphin (4, 8). The recently isolated peptides in this group, urotensin I from two species of teleost fisht, share significant homology with and possess similar biological activities to CRF and sauvagine (9).CRF, sauvagine, and urotensin I belong to a novel family of peptides from widely differing sources. Their high sequence homology is an indication of a possible ancestral relationship. The fact that they are equipotent in some assays indicates that functionally important parts of the molecule were highly conserved during evolution. It is therefore important to establish the secondary and tertiary structures of the three peptides to a...

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“…Peptides were synthesized by the solid-phase approach using protocols described elsewhere (11,12). The peptide content of the lyophilized samples was determined by amino acid analysis.…”

Section: Methodsmentioning

confidence: 99%

Structural homology of corticotropin-releasing factor, sauvagine, and urotensin I: circular dichroism and prediction studies.

Pallai¹,

Mabilia²,

Goodman³

et al. 1983

Proc. Natl. Acad. Sci. U.S.A.

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“…The peptides were assembled on the benzhydrylamine resin or p-methyl benzhydrylamine using dicyclscarbodiimide for coupling of the appropriately protected amino acids at the rate of 10 residues per 24 h (33,34). The protected peptide resin (except for the N-terminus Boc-protecting group which had been removed) was cleaved in hydrofluoric acid and the crude peptide was purified by preparative RP HPLC, using Waters Associates Prep Vydac 15-or 20-pm C-18 silicas.…”

Section: Methodsmentioning

confidence: 99%

Isolation, analysis of structure, synthesis, and biological actions of urotensin I neuropeptides

Lederis¹,

Letter²,

McMaster³

et al. 1983

Can. J. Biochem. Cell Biol.

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The 41-residue neuropeptide urotensin I (UI), from the urophyses of two teleost fish species (Cyprinus carpio and Catostomus commersoni), was isolated and purified, and its amino acid sequence was determined and confirmed by synthesis of a fully active peptide. The UI peptide was found to be a close structural and biological homologue of the ovine hypothalamic corticotropin-releasing factor (CRF) and the frog skin peptide sauvagine; UI is, therefore, a phylogenetic prototype of this group of peptides. Extraction of urophyses in hot acetic or hydrochloric acid cleaves an amino terminal tripeptide yielding a fully active UI(4-41). The UI peptides are equipotent with the other two naturally occurring peptides (CRF and sauvagine) in the release of mammalian pituitary corticotropin (ACTH), but UI is several times more potent than the mammalian homologue in the stimulation of release of fish pituitary ACTH. The UI peptide and its mammalian or amphibian homologues have a long-lasting hypotensive action in mammals, via a uniquely selective vasodilatation in the superior (anterior) mesenteric vascular bed only. The significantly lower hypotensive vasodilatory action of the mammalian homologue (CRF) suggests a change in the unknown physiological role of the haemodynamic actions of the UI peptides in the mammalian gastrointestinal tract during phylogenetic progression from fishes to mammals.

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“…This is partly due to the fact that methionine sulfoxide residues are reduced, and detected as methionines in traditional Edman sequencing procedures [12,13]. In addition, Met oxidation can be artificially introduced during sample preparation, purification and analysis [14,15,20], which presents another degree of complexity in characterization of Met oxidation in proteins.…”

mentioning

confidence: 99%

Detection and characterization of methionine oxidation in peptides by collision-induced dissociation and electron capture dissociation

Guan

Yates

Bakhtiar

2003

J. Am. Soc. Mass Spectrom.

115

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Electron capture dissociation (ECD) and collision-induced dissociation (CID), the two complementary fragmentation techniques, are demonstrated to be effective in the detection and localization of the methionine sulfoxide [Met(O)] residues in peptides using Fourier transform ion cyclotron resonance (FTICR) mass spectrometry. The presence of Met(O) can be easily recognized in the low-energy CID spectrum showing the characteristic loss of methanesulfenic acid (CH 3 SOH, 64 Da) from the side chain of Met(O). The position of Met(O) can then be localized by ECD which is capable of providing extensive peptide backbone fragmentation without detaching the labile Met(O) side chain. We studied CID and ECD of several Met(O)-containing peptides that included the 44-residue human growth hormone-releasing factor (GRF) and the human atrial natriuretic peptide (ANP). The distinction and complementarity of the two fragmentation techniques were particularly remarkable in their effects on ANP, a disulfide bond-containing peptide. While the predominant fragmentation pathway in CID of ANP was the loss of CH 3 SOH (64 Da) from the molecular ion, ECD of ANP resulted in many sequence-informative products, including those from cleavages within the disulfidebonded cyclic structure, to allow for the direct localization of Met(O) without the typical procedures for disulfide bond reduction followed by ™SH alkylation. (J Am Soc Mass Spectrom 2003, 14, 605-613)

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Total solid-phase synthesis of porcine gut gastrin releasing peptide (GRP), a mammalian bombesin

Cited by 78 publications

References 9 publications

Structural homology of corticotropin-releasing factor, sauvagine, and urotensin I: circular dichroism and prediction studies.

Structural homology of corticotropin-releasing factor, sauvagine, and urotensin I: circular dichroism and prediction studies.

Isolation, analysis of structure, synthesis, and biological actions of urotensin I neuropeptides

Detection and characterization of methionine oxidation in peptides by collision-induced dissociation and electron capture dissociation

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