65160-71-6Relevant academic research and scientific papers
A highly effective phosphinite ligand derived from D-mannitol for Rh- catalyzed asymmetric hydrogenation
Chen, Yixin,Li, Xingshu,Tong, Siu-Kuen,Choi, Michael C.K.,Chan, Albert S.C.
, p. 957 - 960 (1999)
A novel chiral phosphinite 1,2,5,6-di-isopropylidene-3, 4- bis(diphenylphosphino)-D-mannitol was prepared and its rhodium complex was found to be an effective catalyst for the asymmetric hydrogenation of amidoacrylic acid and its derivatives with product ee's ranging from 90% to 97%.
New cyclic peptides via ring-closing metathesis reactions and their anti-bacterial activities
Boyle, Timothy P.,Bremner, John B.,Coates, Jonathan,Deadman, John,Keller, Paul A.,Pyne, Stephen G.,Rhodes, David I.
experimental part, p. 11270 - 11290 (2009/04/06)
As part of a program investigating cyclic peptides with an internal aromatic hydrophobic scaffold as potential novel anti-bacterial agents, we explored the synthesis of simple tyrosine-based systems. These were prepared via key intermediates containing internal allylglycine and allyltyrosine residues for subsequent ring-closing metathesis reactions. Although the resulting anti-bacterial activity against Staphylococcus aureus was modest, this represents a novel and simple route to this class of compounds. One intermediate acyclic dipeptide precursor showed good activity against S. aureus with an MIC of 7.8 μg/mL. Crown Copyright
PEPTIDIC COMPOUNDS
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Page/Page column 153, (2008/06/13)
The present invention provides a compound of formula (I), (II), (III) and (IV) as defined herein and pharmaceutically acceptable derivatives thereof. The present invention further provides use of the compounds of the present invention in the treatment of bacterial infection and in the treatment of HIV infection. Also provided are pharmaceutical compositions comprising the compounds of the present invention.
Pronase catalysed peptide syntheses
Lobell, Mario,Schneider, Manfred P.
, p. 319 - 325 (2007/10/03)
A mixture of proteases from Streptomyces griseus (pronase), displaying a very broad substrate tolerance in the hydrolysis of peptides, has been studied for the first time systematically regarding their substrate specificity in peptide synthesis. It is demonstrated that pronase can be employed successfully for the formation of dipeptides with yields up to 95%. Pronase has also been employed successfully as catalyst for the enzyme assisted synthesis of a hexapeptide.
Studies on the Synthesis of Aryl Ethers Using Arene-Manganese Chemistry
Pearson, Anthony J.,Bruhn, Paul R.
, p. 7092 - 7097 (2007/10/02)
Selective arylation of polyfunctional phenols, using chlorobenzene- and p-chlorotoluene-manganese tricarbonyl cations, is described.The intermediate arene-manganese complexes are found to undergo stereo- and regioselective reactions with Schoellkopf's chiral glycine enolate equivalent to give dienyl-Mn(CO)3 complexes.Treatment of these complexes with N-bromosuccinimide at room temperature, followed by hydrolysis of the dihydropyrazine, gives diaryl ethers in which one of the aromatic rings is an arylglycine methyl ester.
N-METHOXYDIACETAMIDE: A NEW SELECTIVE ACETYLATING AGENT
Kikugawa, Yasuo,Mitsui, Kimiyo,Sakamoto, Takeshi,Kawase, Masami,Tamiya, Hiroshi
, p. 243 - 246 (2007/10/02)
A simple and efficient method for the direct chemoselective acetylation of primary amines in the presence of alcohols or secondary amines using a new reagent N-methoxydiacetamide is described.
Octapeptides and methods for their production
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, (2008/06/13)
New octapeptides having the formula Prot Grp-R-Trp-Ser-Tyr-R2 -Leu-Arg-Pro-R3 ; salts thereof; wherein R is Gln, Gln (bzl), His (bzl), Ser (bzl), Pro, Leu, Tyr (bzl), Ile, Cys (bzl) or Phe, R2 is D-Phe, D-Ala, D-Leu, D-Trp, D-Tyr, D-Tyr (Me), D-Ser, D-Met, D-Arg, D-Val, D-His, D-Gln, D-Phs, D-Thr, D-Pro, D-Me5 Phe or D-Asn and R3 is NH2, NH(lower alkyl), N-(lower alkyl)2, NH-benzyl, NHCH2 CH2 N-(lower alkyl)2 or NH-CH2 CH2 SO2 NH-benzyl; methods for their production; certain peptide intermediates and their salts used in the production thereof; and the use of said octapeptides as luteinizing hormone releasing factor antagonists.
