cas 5084-98-0, Z-LEU-GLY-OME | Articles data

Articles about 5084-98-0Total 5 be found

Synthesis of selenoxo peptides and oligoselenoxo peptides employing LiAlHSeH
Synthesis of selenoxo peptides by the treatment of Nα- protected peptide esters with a combination of PCl5 and LiAlHSeH is delineated. The method is simple, high-yielding, and free from racemization. Thus obtained selenoxo peptides are used as units for N-terminal chain extension through Nα-deprotection/coupling to yield peptide-selenoxo peptide hybrids. Multiple selenation is demonstrated by conversion of two peptide bonds of tripeptides into selenoxo peptide bonds. Amino acid derived arylamides are also converted into aryl selenoamides. C6H 5-CSeNH-Val-OMe 8f is obtained as single crystal, and its structure was determined through X-ray diffraction study.
Vishwanatha,Narendra,Chattopadhyay, Basab,Mukherjee, Monika,Sureshbabu, Vommina V.
experimental part
p. 2689 - 2702
(2012/06/01)

Recyclable hypervalent iodine(III) reagent iodosodilactone as an efficient coupling reagent for direct esterification, amidation, and peptide coupling
A hypervalent iodine(III) reagent plays a novel role as an efficient coupling reagent to promote the direct condensation between carboxylic acids and alcohols or amines to provide esters, macrocyclic lactones, amides, as well as peptides without racemization. The regeneration of iodosodilactone (1) can also be readily achieved. The intermediate acyloxyphosphonium ion C from the activation of a carboxylic acid is thought to be involved in the present esterification reaction.
Tian, Jun,Gao, Wen-Chao,Zhou, Dong-Mei,Zhang, Chi
supporting information; experimental part
p. 3020 - 3023
(2012/08/07)

SYNTHESIS OF FRAGMENTS OF THE VP1 PROTEIN OF TYPE A22 FOOT-AND-MOUTH DISEASE VIRUS. SYNTHESIS OF FRAGMENTS 134-139, 134-145, 140-145, 150-155, AND 150-159
Fragments of peptides of the amino acid sequences (134-145) and (150-159) of the VP1 protein of the type A22 foot-and-mouth disease (FMD)virus have been synthesized by the classical methods of peptide chemistry.Oligopeptides were obt
Khalikov, Sh. Kh.,Alieva, S. V.,Ashurov, S. G.
p. 202 - 212
(2007/10/02)

KINETICS OF THE ALKALINE HYDROLYSIS OF SEVERAL N-BENZYLOXYCARBONYLDIPEPTIDE METHYL AND ETHYL ESTERS
The reaction rates of the alkaline hydrolysis of synthesized N-protected dipeptide methyl and ethyl esters were studied systematically.From the kinetic data the energies of activation, the pre-exponential factors and the reference values at 40 deg C were calculated.The rate of hydrolysis shows to be strongly dependent on the C-terminal amino acid in the sequence Gly >> Ala/Met/Phe > Leu >> Val/Pro.Surprisingly the N-terminal amino acid also exerts an effect, but in a different sequence.N-Terminal Phe in particular shows a relative accelerating effect.Remarkable is the significantly faster ester hydrolysis of glycine containing dipeptide ethyl esters in ethanol/water compared to the corresponding methyl esters in methanol/water.
Hoogwater, D. A.,Peereboom, M.
p. 5325 - 5332
(2007/10/02)