95841-14-8Relevant academic research and scientific papers
Fluorinated Pseudopeptide Analogues of the Neuropeptide 26RFa: Synthesis, Biological, and Structural Studies
Pierry, Camille,Couve-Bonnaire, Samuel,Guilhaudis, Laure,Neveu, Cindy,Marotte, Amelie,Lefranc, Benjamin,Cahard, Dominique,Segalas-Milazzo, Isabelle,Leprince, Jerome,Pannecoucke, Xavier
, p. 1620 - 1633 (2013/09/23)
A series of four fluorinated dipeptide analogues each containing a fluoro-olefin moiety as peptide bond surrogate has been designed and synthesized. These motifs have been successfully introduced into the bioactive C-terminal heptapeptide of the neuropeptide 26RFa by conventional SPPS. We then evaluated the ability of the generated pseudopeptides to increase [Ca2+]i in GPR103-transfected cells. For these fluorinated analogues, greater stability in human serum was observed. Their conformations were also investigated, leading to the valuable identification of differences depending on the position of the fluoro-olefin moiety in the sequence.
Aldol reactions between L-erythrulose derivatives and chiral α-amino and α-fluoro aldehydes: Competition between felkin-anh and cornforth transition states
Diaz-Oltra, Santiago,Carda, Miguel,Murga, Juan,Falomir, Eva,Marco, J. Alberto
supporting information; scheme or table, p. 9240 - 9254 (2009/09/30)
Both matched and mismatched diastereoselection have been observed in aldol reactions of a boron enolate of a protected L-erythrulose derivative with several chiral α-fluoro and α-amino aldehydes. Strict adherence to the Felkin-Anh model for the respective transition structures does not account satisfactorily for all the observed results, as previously observed in the case of α-oxygenated aldehydes. In some cases, only the Cornforth model provides a good explanation. The factors that influence this dichotomy are discussed and a general mechanistic model is proposed for aldol reactions with α-heteroatom-substituted aldehydes. Additional support for the model was obtained from density functional calculations.
HETEROCYCLIC PEPTIDE RENIN INHIBITORS
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, (2008/06/13)
A renin inhibiting compound of the formula STR1 wherein X is N, O or CH; R 1 is absent or a functional group; A and L are independently selected from absent, C=O, SO 2 and CH 2 ; D is C=O, SO. sub.2 or CH 2 ; Y is N or CH; R 2 is hydrogen, loweralkyl or substituted alkyl; Z is a functional group; R 3 is loweralkyl or substituted alkyl; n is 0 or 1; and T is a mimic of the Leu-Val cleavage site of angiotensinogen; or a pharmaceutically acceptable salt, ester or prodrug thereof.
Renin inhibitors having all retro-inverted peptide bonds
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, (2008/06/13)
Renin-inhibiting peptides of the formula STR1 in which X represents a group of the formula STR2 represents hydroxyl, alkoxy having up to 8 carbon atoms, benzyloxy or a group of the formula --NR4 R5, A, B, D and E are identical or different and in each case represent a direct bond, represent a radical of the formula STR3 in which Q1 denotes oxygen, sulphur or the methylene group represent a grouping of the formula STR4 m represents a number 0, 1 or 2, and L represents a group of the formula --CH2 NR2 R3 and physiologically acceptable salts thereof.
