Bradykinin-related peptides from Phyllomedusa hypochondrialis

Brand, Guilherme D.; Krause, Friedemann; Silva, Luciano; Leite, José Roberto S. A.; Melo, Jorge Alex Taquita; Prates, Maura V.; Pesquero, João Bosco; Santos, Edson Lucas dos; Nakaie, Clóvis R.; Costa-Neto, Cláudio M.; Bloch, Carlos

doi:10.1016/j.peptides.2006.04.020

Cited by 58 publications

(52 citation statements)

References 22 publications

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“…Recombinat MtCDA was analyzed by MALDI-TOF/TOF on an ABI 4700 Proteomics Analyzer (Applied Biosystems, Framingham, MA, USA), an Ultraflex II (Bruker Daltonics, Germany) and a Q-TOF Ultima API (Micromass, UK) as described elsewhere (Brand et al, 2006).…”

Section: Mass Spectrometry Analysismentioning

confidence: 99%

See 1 more Smart Citation

Structural and functional analyses of Mycobacterium tuberculosis Rv3315c-encoded metal-dependent homotetrameric cytidine deaminase

Sánchez-Quitian

Schneider

Ducati

et al. 2010

Journal of Structural Biology

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The emergence of drug-resistant strains of Mycobacterium tuberculosis, the causative agent of tuberculosis, has exacerbated the treatment and control of this disease. Cytidine deaminase (CDA) is a pyrimidine salvage pathway enzyme that recycles cytidine and 2'-deoxycytidine for uridine and 2'-deoxyuridine synthesis, respectively. A probable M. tuberculosis CDA-coding sequence (cdd, Rv3315c) was cloned, sequenced, expressed in Escherichia coli BL21(DE3), and purified to homogeneity. Mass spectrometry, N-terminal amino acid sequencing, gel filtration chromatography, and metal analysis of M. tuberculosis CDA (MtCDA) were carried out. These results and multiple sequence alignment demonstrate that MtCDA is a homotetrameric Zn(2+)-dependent metalloenzyme. Steady-state kinetic measurements yielded the following parameters: K(m)=1004 microM and k(cat)=4.8s(-1) for cytidine, and K(m)=1059 microM and k(cat)=3.5s(-1) for 2'-deoxycytidine. The pH dependence of k(cat) and k(cat)/K(M) for cytidine indicate that protonation of a single ionizable group with apparent pK(a) value of 4.3 abolishes activity, and protonation of a group with pK(a) value of 4.7 reduces binding. MtCDA was crystallized and crystal diffracted at 2.0 A resolution. Analysis of the crystallographic structure indicated the presence of a Zn(2+) coordinated by three conserved cysteines and the structure exhibits the canonical cytidine deaminase fold.

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Section: Mass Spectrometry Analysismentioning

confidence: 99%

“…N-terminal amino acid residues of recombinant homogeneous MtCDA were determined by automated Edman degradation sequencing using a PPSQ 23 protein peptide sequencer (Shimadzu Co., Japan) (Brand et al, 2006).…”

Section: N-terminal Amino Acid Sequencingmentioning

confidence: 99%

Structural and functional analyses of Mycobacterium tuberculosis Rv3315c-encoded metal-dependent homotetrameric cytidine deaminase

Sánchez-Quitian

Schneider

Ducati

et al. 2010

Journal of Structural Biology

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“…The N-terminal amino acid residues of homogeneous rhGM-CSF were identified by the automated Edman degradation method on a PPSQ-23 protein peptide sequencer (Shimadzu Co., Japan) as described elsewhere [21].…”

Section: N-terminal Amino Acid Sequencingmentioning

confidence: 99%

Molecular cloning, expression in Escherichia coli and production of bioactive homogeneous recombinant human granulocyte and macrophage colony stimulating factor

Schwanke

Renard

Chies

et al. 2009

International Journal of Biological Macromolecules

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“…Moreover, some amphibian secretions contain a number of small proteins and a large number of peptide components whose biological functions are still undetermined. Several peptides from skin secretions of amphibians, more particularly tree-frogs, have been purified in recent years, including antimicrobial peptides, bradykinin related peptides and one bradykinin-potentiating peptide (BPP) (5)(6)(7)(8)(9).…”

Section: Introductionmentioning

confidence: 99%

Identification of bradykinin: related peptides from Phyllomedusa nordestina skin secretion using electrospray ionization tandem mass spectrometry after a single-step liquid chromatography

Conceição¹,

Bruni²,

Sciani³

et al. 2009

J. Venom. Anim. Toxins incl. Trop. Dis

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ABSTRACT:Amphibian skin secretions are a source of potential new drugs with medical and biotechnological applications. Rich in peptides produced by holocrinetype serous glands in the integument, these secretions play different roles, either in the regulation of physiological skin functions or in the defense against predators or microorganisms. The aim of the present work was to identify novel peptides with bradykinin-like structure and/or activity present in the skin of Phyllomedusa nordestina. In order to achieve this goal, the crude skin secretion of this frog was prefractionated by solid phase extraction and separated by reversed-phase chromatography. The fractions were screened for low-molecular-mass peptides and sequenced by mass spectrometry. It was possible to identify three novel bradykininrelated peptides, namely: KPLWRL-NH 2 (Pnor 3), RPLSWLPK (Pnor 5) and VPPKGVSM (Pnor 7) presenting vascular activities as assessed by intravital microscopy. Pnor 3 and Pnor 7 were able to induce vasodilation. On the other hand, Pnor 5 was a potent vasoconstrictor. These effects were reproduced by their synthetic analogues.

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Bradykinin-related peptides from Phyllomedusa hypochondrialis

Cited by 58 publications

References 22 publications

Structural and functional analyses of Mycobacterium tuberculosis Rv3315c-encoded metal-dependent homotetrameric cytidine deaminase

Structural and functional analyses of Mycobacterium tuberculosis Rv3315c-encoded metal-dependent homotetrameric cytidine deaminase

Molecular cloning, expression in Escherichia coli and production of bioactive homogeneous recombinant human granulocyte and macrophage colony stimulating factor

Identification of bradykinin: related peptides from Phyllomedusa nordestina skin secretion using electrospray ionization tandem mass spectrometry after a single-step liquid chromatography

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