Data

Peptides that inhibit neuronal nitric oxide synthase

Australian Institute of Marine Science
Australian Institute of Marine Science (AIMS)
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ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Adc&rfr_id=info%3Asid%2FANDS&rft_id=https://apps.aims.gov.au/metadata/view/71ffe97b-efec-4814-a657-4240fef7cae2&rft.title=Peptides that inhibit neuronal nitric oxide synthase&rft.identifier=https://apps.aims.gov.au/metadata/view/71ffe97b-efec-4814-a657-4240fef7cae2&rft.publisher=Australian Institute of Marine Science (AIMS)&rft.description=Neuronal nitric oxide synthase (nNOS) inhibition tests were carried out on peptides in addition to other bioactivity experiments, in particular, antibiotic activity. Inhibition of nNOS was measured by monitoring the conversion of [3H]arginine to [3H]citrulline.Information recorded: individual identifier for sample, peptide sequence, molecular weight, stock concentration (mg/ml), source (native peptide, synthetic derivative), solvent and concentration. To test whether the peptides inhibit nNOS. Peptides tested: aurein, caerin, citropin, cupiennin, dahlein, frenatin, lesueurin, rothein, signiferin, uperin.Sources of native peptides: Cirinia signifera; Cupiennius salei; Litoria aurea, L. caerulea, L. citropa, L. chloris, L. dahlii, L. electrica, L. gilleni, L. gracilenta, L. infrafrenata, L. lesueuri, L. rothii, L. rubella, L. splendida, hybrid L. caerulea/splendida; Uperoleia mjobergii.The first report of neuronal nitric oxide synthase inhibition by a component of a spider venom (Cupiennius salei).Subsets of the data have been used in a number of studies.Maintenance and Update Frequency: notPlanned&rft.creator=Australian Institute of Marine Science (AIMS) &rft.date=2025&rft_rights=Creative Commons Attribution-NonCommercial 3.0 Australia License http://creativecommons.org/licenses/by-nc/3.0/au/&rft_rights=Use Limitation: All AIMS data, products and services are provided as is and AIMS does not warrant their fitness for a particular purpose or non-infringement. While AIMS has made every reasonable effort to ensure high quality of the data, products and services, to the extent permitted by law the data, products and services are provided without any warranties of any kind, either expressed or implied, including without limitation any implied warranties of title, merchantability, and fitness for a particular purpose or non-infringement. AIMS make no representation or warranty that the data, products and services are accurate, complete, reliable or current. To the extent permitted by law, AIMS exclude all liability to any person arising directly or indirectly from the use of the data, products and services.&rft_rights=Attribution: Format for citation of metadata sourced from Australian Institute of Marine Science (AIMS) in a list of reference is as follows: Australian Institute of Marine Science (AIMS). (2009). Peptides that inhibit neuronal nitric oxide synthase. https://apps.aims.gov.au/metadata/view/71ffe97b-efec-4814-a657-4240fef7cae2, accessed[date-of-access].&rft_rights=Resource Usage:Use of the AIMS data is for not-for-profit applications only. All other users shall seek permission for use by contacting AIMS. Acknowledgements as prescribed must be clearly set out in the user's formal communications or publications.Access Constraint: intellectualPropertyRightsUse Constraint: intellectualPropertyRightsSecurity classification code: unclassifiedMetadata Usage:Access Constraint: intellectualPropertyRightsUse Constraint: intellectualPropertyRightsSecurity classification code: unclassified&rft_subject=oceans&rft.type=dataset&rft.language=English Access the data
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Creative Commons Attribution-NonCommercial 3.0 Australia License
http://creativecommons.org/licenses/by-nc/3.0/au/

Use Limitation: All AIMS data, products and services are provided "as is" and AIMS does not warrant their fitness for a particular purpose or non-infringement. While AIMS has made every reasonable effort to ensure high quality of the data, products and services, to the extent permitted by law the data, products and services are provided without any warranties of any kind, either expressed or implied, including without limitation any implied warranties of title, merchantability, and fitness for a particular purpose or non-infringement. AIMS make no representation or warranty that the data, products and services are accurate, complete, reliable or current. To the extent permitted by law, AIMS exclude all liability to any person arising directly or indirectly from the use of the data, products and services.

Attribution: Format for citation of metadata sourced from Australian Institute of Marine Science (AIMS) in a list of reference is as follows: "Australian Institute of Marine Science (AIMS). (2009). Peptides that inhibit neuronal nitric oxide synthase. https://apps.aims.gov.au/metadata/view/71ffe97b-efec-4814-a657-4240fef7cae2, accessed[date-of-access]".

Resource Usage:Use of the AIMS data is for not-for-profit applications only. All other users shall seek permission for use by contacting AIMS. Acknowledgements as prescribed must be clearly set out in the user's formal communications or publications.Access Constraint: intellectualPropertyRightsUse Constraint: intellectualPropertyRightsSecurity classification code: unclassifiedMetadata Usage:Access Constraint: intellectualPropertyRightsUse Constraint: intellectualPropertyRightsSecurity classification code: unclassified

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Neuronal nitric oxide synthase (nNOS) inhibition tests were carried out on peptides in addition to other bioactivity experiments, in particular, antibiotic activity. Inhibition of nNOS was measured by monitoring the conversion of [3H]arginine to [3H]citrulline.Information recorded: individual identifier for sample, peptide sequence, molecular weight, stock concentration (mg/ml), source (native peptide, synthetic derivative), solvent and concentration.
To test whether the peptides inhibit nNOS.
Peptides tested: aurein, caerin, citropin, cupiennin, dahlein, frenatin, lesueurin, rothein, signiferin, uperin.Sources of native peptides: Cirinia signifera; Cupiennius salei; Litoria aurea, L. caerulea, L. citropa, L. chloris, L. dahlii, L. electrica, L. gilleni, L. gracilenta, L. infrafrenata, L. lesueuri, L. rothii, L. rubella, L. splendida, hybrid L. caerulea/splendida; Uperoleia mjobergii.The first report of neuronal nitric oxide synthase inhibition by a component of a spider venom (Cupiennius salei).Subsets of the data have been used in a number of studies.

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Maintenance and Update Frequency: notPlanned

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Credit
Doyle, Jason R, Mr (Custodian)

Modified: 19 09 2025

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Cupiennin 1a, an antimicrobial peptide from the venom of the neotropical wandering spider Cupiennius salei, also inhibits the formation of nitric oxide by neuronal nitric oxide synthase: Pukala TL, Doyle JR, Llewellyn LE, Kuhn-Nentwig L, Apponyi MA, Separovic F and Bowie JH (2007) Cupiennin 1a, an antimicrobial peptide from the venom of the neotropical wandering spider Cupiennius salei, also inhibits the formation of nitric oxide by neuronal nitric oxide synthase. FEBS Journal 274(7):1778-1784.

local : articleId=7399

Host-defence peptide profiles of the skin secretions of interspecific hybrid tree frogs and their parents, female Litoria splendida and male Litoria caerulea: Pukala TL, Bowie JH, Bertozzi T, Donnellan SC, Doyle JR, Surinya-Johnson KH, Liu Y, Jackway RJ, Llewellyn LE and Tyler MJ (2006) Host-defence peptide profiles of the skin secretions of interspecific hybrid tree frogs and their parents, female Litoria splendida and male Litoria caerulea. FEBS Journal 273:3511-3519.

local : articleId=7235

nNOS inhibition, antimicrobial and anticancer activity of the amphibian skin peptide, citropin 1.1 and synthetic modifications. The solution structure of a modified citropin 1.1: Doyle JR, Brinkworth CS, Wegener KL, Carver JA, Llewellyn LE, Oliver IN, Bowie JH, Wabnitz PA and Tyler MJ (2003) nNOS inhibition, antimicrobial and anticancer activity of the amphibian skin peptide, citropin 1.1 and synthetic modifications. The solution structure of a modified citropin 1.1. European Journal of Biochemistry 270: 1141-1153.

local : articleId=6401

The solution structure of frenatin 3, an nNOS inhibitor from the giant tree frog Litoria infrafrenata: Brinkworth CS, Carver JA, Wegener KL, Doyle JR, Llewellyn LE and Bowie JH (2003) The solution structure of frenatin 3, an nNOS inhibitor from the giant tree frog Litoria infrafrenata. Biopolymers 70: 424-434.

local : articleId=6585

New caerin antibiotic peptides from the skin secretion of the Dainty Green Tree Frog Litoria gracilenta. Identification using positive and negative ion electrospray mass spectrometry: Maclean MJ, Brinkworth CS, Bilusich D, Bowie JH, Llewellyn LE, Doyle JR and Tyler MJ (2006) New caerin antibiotic peptides from the skin secretion of the Dainty Green Tree Frog Litoria gracilenta. Identification using positive and negative ion electrospray mass spectrometry. Toxicon 47:664-675.

local : articleId=7227

Amphibian peptides that inhibit neuronal nitric oxide synthase. The isolation of lesueurin from the skin secretion of the Australian Stony Creek frog Litoria lesueuri: Doyle JR, Llewellyn LE, Brinkworth C, Bowie JH, Wegener KL, Rozek T, Wabnitz PA, Wallace JC and Tyler MJ (2002) Amphibian peptides that inhibit neuronal nitric oxide synthase. The isolation of lesueurin from the skin secretion of the Australian Stony Creek frog Litoria lesueuri. European Journal of Biochemistry 269: 100-109.

local : articleId=6172

Identifiers
  • global : 71ffe97b-efec-4814-a657-4240fef7cae2