P.-A. Jaquenoud

Bio: P.-A. Jaquenoud is an academic researcher from University of Geneva. The author has contributed to research in topics: Bradykinin & Bradykinin receptor. The author has an hindex of 12, co-authored 14 publications receiving 870 citations.

Une nouvelle synthèse de l'oxytocine

Abstract: A new synthesis of oxytocin is described. N-CBO-L-glutaminyl-L-asparaginyl-S-benzyl-L-cysteinyl-azide is reacted with L-prolyl-L-leucyl-glycinamide to give N-CBO-L- glutaminyl-L-asparaginyl-S-benzyl-L-cysteinyl-L-prolyl-L-leucyl-glycinamide. After removal of the CBO group by HBr in acetic acid this hexapeptide is condensed with N-CBO-S-benzyl-L-cysteinyl-L-tyrosyl-L-isoleucyl-azide to give the nonapeptide N-CBO-S-benzyl-L-cysteinyl-L-tyrosyl-L- isoleucyl-L-glutaminyl-L-asparaginyl-S-benzyl-L-cysteinyl-L-prolyl-L-leucyl-glycinamide already obtained by du Vigneaud and coworkers through another route. Reduction with sodium in liquid ammonia and reoxydation gives biologically active material.

Synthèse de la L-arginyl-L-prolyl-L-prolyl-glycyl-L-phénylalanyl-L-Séryl-L-prolyl-L-phénylalanyl-L-arginine, un nonapeptide présentant les propriétés de la bradykinine

Abstract: The synthesis of a nonapeptide exhibiting bradykinin-like properties is described. Condensation of CBO-(nitro)Arg-Pro-OH with H-Pro-Gly-NHNH-CTO and selective splitting of the CTO-group yielded CBO-(nitro)Arg-Pro-Pro-Gly-NHNH2. CBO-Phe- Ser-N2 was condensed with H-Pro-Phe-(nitro)Arg-OBzN, the CBO-group was selectively split, and the resulting pentapeptide was made to react with the azide corresponding to the above-mentioned hydrazide. All the protective groups of the resulting nonapeptide were split off by catalytic hydrogenolysis, giving pure H-Arg- Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg-OH after counter-current distribution. On a molar basis, this nonapeptide was more active than histamine (ileum, bronchial muscle and capillary permeability of the guinea pig) and acetylcholine (duodenum of the rabbit, blood pressure of the rabbit and dog).

Synthèse de la L‐histidyl‐L‐phénylalanyl‐L‐arginyl‐L‐tryptophanyl‐glycyl‐ϵ‐CBO‐L‐lysyl‐L‐prolyl‐L‐valylamide

Abstract: Trityl-glycyl-ϵ-CBO-L-lysine is condensed with L-prolyl-L-valine methyl ester and, after amidification and splitting of the trityl group, glycyl-ϵ-CBO-L-lysyl-L-prolyl-L-valylamide is obtained This is condensed with ditrityl-L-histidyl-L-phenylalanyl-L-arginyl-L-tryptophane prepared by condensation of ditrityl-L-histidyl-L-phenylalanine with L-arginyl-L-tryptophane methyl ester and saponification Dicyclohexyl-carbodiimide is used as a condensing agent After splitting off the trityl groups, the final octapeptide, L-histidyl-L-phenylalanyl-L-arginyl-L-tryptophanyl-glycyl-ϵ-CBO-L-lysyl-L-prolyl-L-valylamide is shown to be optically pure by leucine-aminopeptidase digestion

Synthesis and biological activity of peptides related to bradykinin.

Abstract: Die Synthese von 6 Polypeptiden aus den im Bradykinin vorkommenden Aminosauren wird beschrieben. Das Nonapeptid H-l-Arg-l-Pro-l-Pro-Gly-l-Phe-l-Ser-l-Pro-l-Phe-l-Arg-OH zeigte hohe Bradykinin-ahnliche Wirksamkeit in verschiedenen biologischen Testen.

Synthèse d'analogues structuraux de l'oxytocine

Abstract: The syntheses of four analogues of oxytocine are described: one with a phenylalanyl residue replacing the isoleucyl residue, one with a leucyl residue replacing the isoleucyl residue, one with a valyl residue replacing the isoleucyl residue, and one with a glutaminyl residue replacing the asparaginyl residue.

International Union of Pharmacology. XLV. Classification of the Kinin Receptor Family: from Molecular Mechanisms to Pathophysiological Consequences

Abstract: Kinins are proinflammatory peptides that mediate numerous vascular and pain responses to tissue injury. Two pharmacologically distinct kinin receptor subtypes have been identified and characterized for these peptides, which are named B1 and B2 and belong to the rhodopsin family of G protein-coupled receptors. The B2 receptor mediates the action of bradykinin (BK) and lysyl-bradykinin (Lys-BK), the first set of bioactive kinins formed in response to injury from kininogen precursors through the actions of plasma and tissue kallikreins, whereas the B(1) receptor mediates the action of des-Arg9-BK and Lys-des-Arg9-BK, the second set of bioactive kinins formed through the actions of carboxypeptidases on BK and Lys-BK, respectively. The B2 receptor is ubiquitous and constitutively expressed, whereas the B1 receptor is expressed at a very low level in healthy tissues but induced following injury by various proinflammatory cytokines such as interleukin-1beta. Both receptors act through G alpha(q) to stimulate phospholipase C beta followed by phosphoinositide hydrolysis and intracellular free Ca2+ mobilization and through G alpha(i) to inhibit adenylate cyclase and stimulate the mitogen-activated protein kinase pathways. The use of mice lacking each receptor gene and various specific peptidic and nonpeptidic antagonists have implicated both B1 and B2 receptors as potential therapeutic targets in several pathophysiological events related to inflammation such as pain, sepsis, allergic asthma, rhinitis, and edema, as well as diabetes and cancer. This review is a comprehensive presentation of our current understanding of these receptors in terms of molecular and cell biology, physiology, pharmacology, and involvement in human disease and drug development.