Probing the bradykinin receptor: Mapping the geometric topography using ethers of hydroxyproline in novel peptides

D. J. Kyle; J. A. Martin; R. M. Burch; J. P. Carter; S. Lu; S. Meeker; J. C. Prosser; J. P. Sullivan; J. Togo; L. Noronha-Blob; J. A. Sinsko; R. F. Walters; L. W. Whaley; R. N. Hiner

doi:10.1007/978-3-0348-7321-5_63

Probing the bradykinin receptor: Mapping the geometric topography using ethers of hydroxyproline in novel peptides

D. J. Kyle, J. A. Martin, R. M. Burch, J. P. Carter, S. Lu, S. Meeker, J. C. Prosser, J. P. Sullivan, J. Togo, L. Noronha-Blob, J. A. Sinsko, R. F. Walters, L. W. Whaley, R. N. Hiner

Research output: Contribution to journal › Article › peer-review

1 Scopus citations

Abstract

Five decapeptides were prepared, each having the generic primary sequence D-Arg⁰-Arg¹-Pro²-Hyp³-Gly⁴-Thi⁵-Ser⁶-X⁷-Y⁸-Arg⁹. A C-terminal β-turn was anticipated when X was an alkyl ether of D-4-hydroxyproline in either the cis or trans geometric state and Y was either a Tic or Oic residue. Whereas cis ethers have only very weak receptor affinities, the trans ethers are signifcantly more potent in binding to guinea pig smooth muscle having K(i) values as low as 0.16 nM. Notably, these peptides do not contain a D-aromatic amino acid at position 7 of the primary sequence.

Original language	English (US)
Pages (from-to)	513-525
Number of pages	13
Journal	Agents and Actions
Volume	38
Issue number	SUPPL. I
DOIs	https://doi.org/10.1007/978-3-0348-7321-5_63
State	Published - 1992
Externally published	Yes

ASJC Scopus subject areas

Toxicology
Pharmacology (medical)

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Kyle, D. J., Martin, J. A., Burch, R. M., Carter, J. P., Lu, S., Meeker, S., Prosser, J. C., Sullivan, J. P., Togo, J., Noronha-Blob, L., Sinsko, J. A., Walters, R. F., Whaley, L. W., & Hiner, R. N. (1992). Probing the bradykinin receptor: Mapping the geometric topography using ethers of hydroxyproline in novel peptides. Agents and Actions, 38(SUPPL. I), 513-525. https://doi.org/10.1007/978-3-0348-7321-5_63

Kyle, DJ, Martin, JA, Burch, RM, Carter, JP, Lu, S, Meeker, S, Prosser, JC, Sullivan, JP, Togo, J, Noronha-Blob, L, Sinsko, JA, Walters, RF, Whaley, LW & Hiner, RN 1992, 'Probing the bradykinin receptor: Mapping the geometric topography using ethers of hydroxyproline in novel peptides', Agents and Actions, vol. 38, no. SUPPL. I, pp. 513-525. https://doi.org/10.1007/978-3-0348-7321-5_63

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title = "Probing the bradykinin receptor: Mapping the geometric topography using ethers of hydroxyproline in novel peptides",

abstract = "Five decapeptides were prepared, each having the generic primary sequence D-Arg0-Arg1-Pro2-Hyp3-Gly4-Thi5-Ser6-X7-Y8-Arg9. A C-terminal β-turn was anticipated when X was an alkyl ether of D-4-hydroxyproline in either the cis or trans geometric state and Y was either a Tic or Oic residue. Whereas cis ethers have only very weak receptor affinities, the trans ethers are signifcantly more potent in binding to guinea pig smooth muscle having K(i) values as low as 0.16 nM. Notably, these peptides do not contain a D-aromatic amino acid at position 7 of the primary sequence.",

author = "Kyle, {D. J.} and Martin, {J. A.} and Burch, {R. M.} and Carter, {J. P.} and S. Lu and S. Meeker and Prosser, {J. C.} and Sullivan, {J. P.} and J. Togo and L. Noronha-Blob and Sinsko, {J. A.} and Walters, {R. F.} and Whaley, {L. W.} and Hiner, {R. N.}",

year = "1992",

doi = "10.1007/978-3-0348-7321-5_63",

language = "English (US)",

volume = "38",

pages = "513--525",

journal = "Agents and Actions",

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T1 - Probing the bradykinin receptor

T2 - Mapping the geometric topography using ethers of hydroxyproline in novel peptides

AU - Kyle, D. J.

AU - Martin, J. A.

AU - Burch, R. M.

AU - Carter, J. P.

AU - Lu, S.

AU - Meeker, S.

AU - Prosser, J. C.

AU - Sullivan, J. P.

AU - Togo, J.

AU - Noronha-Blob, L.

AU - Sinsko, J. A.

AU - Walters, R. F.

AU - Whaley, L. W.

AU - Hiner, R. N.

PY - 1992

Y1 - 1992

N2 - Five decapeptides were prepared, each having the generic primary sequence D-Arg0-Arg1-Pro2-Hyp3-Gly4-Thi5-Ser6-X7-Y8-Arg9. A C-terminal β-turn was anticipated when X was an alkyl ether of D-4-hydroxyproline in either the cis or trans geometric state and Y was either a Tic or Oic residue. Whereas cis ethers have only very weak receptor affinities, the trans ethers are signifcantly more potent in binding to guinea pig smooth muscle having K(i) values as low as 0.16 nM. Notably, these peptides do not contain a D-aromatic amino acid at position 7 of the primary sequence.

AB - Five decapeptides were prepared, each having the generic primary sequence D-Arg0-Arg1-Pro2-Hyp3-Gly4-Thi5-Ser6-X7-Y8-Arg9. A C-terminal β-turn was anticipated when X was an alkyl ether of D-4-hydroxyproline in either the cis or trans geometric state and Y was either a Tic or Oic residue. Whereas cis ethers have only very weak receptor affinities, the trans ethers are signifcantly more potent in binding to guinea pig smooth muscle having K(i) values as low as 0.16 nM. Notably, these peptides do not contain a D-aromatic amino acid at position 7 of the primary sequence.

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JO - Agents and Actions

JF - Agents and Actions

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ER -

Probing the bradykinin receptor: Mapping the geometric topography using ethers of hydroxyproline in novel peptides

Abstract

ASJC Scopus subject areas

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