Anantin-A peptide antagonist of the atrial natriuretic factor(ANF). I. Producing organism, fermentation, isolation and biological activity.

Weber, Wolfgang; Fischli, Walter; Hochuli, Erich; Kupfer, Ernst; Weibel, E. K.

doi:10.7164/antibiotics.44.164

Cited by 107 publications

(88 citation statements)

References 13 publications

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“…They form three classes depending on the absence (class II) or presence of one (class III) or two (class I) disulfide bridges that further stabilize the structure [6]. They exhibit a variety of biological activities, involving enzyme inhibition, receptor antagonism, antimicrobial or anti-HIV activities (see Table 1 for class II lasso peptides) [5,[7][8][9][10][11][12]. Their compact structure confers to lasso peptides a great resistance to denaturing conditions and certain proteases.…”

Section: Introductionmentioning

confidence: 99%

Topoisomer Differentiation of Molecular Knots by FTICR MS: Lessons from Class II Lasso Peptides

Zirah

Afonso

Linne

et al. 2011

J. Am. Soc. Mass Spectrom.

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Lasso peptides constitute a class of bioactive peptides sharing a knotted structure where the C-terminal tail of the peptide is threaded through and trapped within an N-terminal macrolactam ring. The structural characterization of lasso structures and differentiation from their unthreaded topoisomers is not trivial and generally requires the use of complementary biochemical and spectroscopic methods. Here we investigated two antimicrobial peptides belonging to the class II lasso peptide family and their corresponding unthreaded topoisomers: microcin J25 (MccJ25), which is known to yield two-peptide product ions specific of the lasso structure under collisioninduced dissociation (CID), and capistruin, for which CID does not permit to unambiguously assign the lasso structure. The two pairs of topoisomers were analyzed by electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry (ESI-FTICR MS) upon CID, infrared multiple photon dissociation (IRMPD), and electron capture dissociation (ECD). CID and ECD spectra clearly permitted to differentiate MccJ25 from its non-lasso topoisomer MccJ25-Icm, while for capistruin, only ECD was informative and showed different extent of hydrogen migration (formation of c•/z from c/z • ) for the threaded and unthreaded topoisomers. The ECD spectra of the triply-chargedMccJ25 and MccJ25-lcm showed a series of radical b-type product ions ðb 0 I n Þ. We proposed that these ions are specific of cyclic-branched peptides and result from a dual c/z • and y/b dissociation, in the ring and in the tail, respectively. This work shows the potentiality of ECD for structural characterization of peptide topoisomers, as well as the effect of conformation on hydrogen migration subsequent to electron capture.

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Section: Introductionmentioning

confidence: 99%

Topoisomer Differentiation of Molecular Knots by FTICR MS: Lessons from Class II Lasso Peptides

Zirah

Afonso

Linne

et al. 2011

J. Am. Soc. Mass Spectrom.

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“…Propeptin competitively inhibits the enzyme activity of prolyl endopeptidase (Kiϭ0.7 m M) and also has antimicrobial activity against Mycobacterium phlei IFO3158 (Inhibition zoneϭ12ϳ15 mm at 40 mg/disc) [6,9]. Peptide compounds similar to propeptin have been reported, including anantins (Gly-Asp type) [10,11], RES-701s (Gly-Asp type)…”

mentioning

confidence: 99%

Novel Propeptin Analog, Propeptin-2, Missing Two Amino Acid Residues from the Propeptin C-Terminus Loses Antibiotic Potency

et al. 2007

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A novel inhibitor of prolyl endopeptidase, the propeptin analog propeptin-2 (C 105 H 130 N 24 O 24 ), missing two amino acid residues from the propeptin C-terminus was isolated from the fermentation broth of propeptinproducing Microbispora sp. SNA-115 grown using a large inoculum. It shows the same enzyme inhibition activity as propeptin against prolyl endopeptidase (Kiϭ1.5 m M), but its antimicrobial activity against Mycobacterium phlei is more than 100-fold lower.Keywords propeptin, Microbispora sp., Mycobacterium spp., prolyl endopeptidase Prolyl endopeptidase (PEP; post-proline cleaving enzyme; official name: prolyl oligopeptidase; EC 3.4.21.26) cleaves peptide bonds at the carboxyl side of proline residues and hydrolyzes biologically active peptides containing proline, such as vasopressin and substance P [1,2]. It may also be involved in diseases such as Alzheimer's disease and bipolar affective disorder [3ϳ5]. Meanwhile, effective antituberculosis drugs with novel structures and mechanisms of action have not been developed in over 30 years. Moreover, the increase in Human Immunodeficiency Virus (HIV) and cancer patients has resulted in the spread of opportunistic bacteria, such as the Mycobacterium avium complex (MAC).Propeptin ( Fig. 1(a)

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“…A 30-min equilibration period was followed by an 80-min sampling period. The sampling period consisted of a 30-min control basal period, a 20-min period, during which ANP (Bachem; King of Prussia, PA) was superfused at various concentrations (0.1 pM to 0.1 M) either alone or in combination with the competitive NPR-A receptor antagonist anantin (Bachem) (5,17,32) or the axonal blocker tetrodotoxin, and a final 30-min control period. In some experiments, somatostatin antibody (S775, raised by A. Arimura; final dilution 1:300) or normal rabbit serum (final dilution 1:300) was superfused for 30 min before superfusion with ANP (10 nM).…”

Section: Methodsmentioning

confidence: 99%

Gastric atrial natriuretic peptide regulates endocrine secretion in antrum and fundus of human and rat stomach

Gower

Premaratne

McCuen

et al. 2003

American Journal of Physiology-Gastrointestinal and Liver Physi

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. Gastric atrial natriuretic peptide regulates endocrine secretion in antrum and fundus of human and rat stomach. Am J Physiol Gastrointest Liver Physiol 284: G638-G645, 2003; 10.1152/ajpgi. 00427.2002-Atrial natriuretic peptide (ANP) is present in gastric mucosa and preferentially binds to two subtypes of natriuretic peptide receptors (NPR), NPR-A and NPR-C. The present study examines the role of endogenous ANP in regulating endocrine secretion in rat and human stomachs. NPR-A protein expression and transcripts were identified in rat antral and fundic mucosa by Western blot and RT-PCR. In superfused rat and human antral and fundic segments, ANP (0.1 pM to 0.1 M) caused a concentration-dependent increase in somatostatin secretion. In antrum, this was accompanied by a decrease in gastrin, and in fundus, this was accompanied by a decrease in histamine secretion. Changes in gastrin and histamine secretion reflected changes in somatostatin secretion and were abolished by somatostatin antibody. The NPR-A receptor antagonist anantin 1) inhibited basal somatostatin secretion and 2) abolished the somatostatin, gastrin, and histamine responses to ANP. We conclude that endogenous ANP, acting via the NPR-A receptor, stimulates somatostatin secretion from both antrum and fundus of rat and human stomach. Stimulation of somatostatin secretion is coupled to inhibition of gastrin secretion in the antrum and inhibition of histamine secretion in the fundus.

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Anantin-A peptide antagonist of the atrial natriuretic factor(ANF). I. Producing organism, fermentation, isolation and biological activity.

Cited by 107 publications

References 13 publications

Topoisomer Differentiation of Molecular Knots by FTICR MS: Lessons from Class II Lasso Peptides

Topoisomer Differentiation of Molecular Knots by FTICR MS: Lessons from Class II Lasso Peptides

Novel Propeptin Analog, Propeptin-2, Missing Two Amino Acid Residues from the Propeptin C-Terminus Loses Antibiotic Potency

Gastric atrial natriuretic peptide regulates endocrine secretion in antrum and fundus of human and rat stomach

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