120341-32-4Relevant academic research and scientific papers
A convenient and rapid method for the selective oxygen-17 enrichment of aspartyl peptides during solid-phase synthesis
Theodorou-Kassioumis, Vassiliki,Biris, Nikolaos,Sakarellos, Constantinos,Tsikaris, Vassilios
, p. 7703 - 7705 (2001)
In this work we describe, for the first time, a rapid and efficient method for 17O selective labeling on the β-carboxyl group of an aspartic acid residue already incorporated into a peptide sequence anchored on a solid-phase support. The β-O-benzyl ester of the Asp residue of the Ac-RGD-benzydrylamine resin was successfully saponified using Na17OH in a methanol/dichloromethane mixture. The 17O selective enriched peptide was then released from the solid support by acidic cleavage. The 17O NMR spectrum confirmed the 17O labeling of the Asp β-carboxylate.
Morphological control of self-assembled multivalent (SAMul) heparin binding in highly competitive media
Rodrigo, Ana C.,Bromfield, Stephen M.,Laurini, Erik,Posocco, Paola,Pricl, Sabrina,Smith, David K.
, p. 6335 - 6338 (2017)
Tuning molecular structures of self-assembling multivalent (SAMul) dendritic cationic lipopeptides controls the self-assembled morphology. In buffer, spherical micelles formed by higher generation systems bind polyanionic heparin better than worm-like micelles formed by lower generation systems. In human serum, the binding of spherical micelles to heparin is adversely affected, while worm-like micelles maintain their relative binding ability.
N-linked peptidoresorc[4]arene-based receptors as noncompetitive inhibitors for α-chymotrypsin
Dacquarica, Ilaria,Cerreto, Antonella,Delle Monache, Giuliano,Subrizi, Fabiana,Boffi, Alberto,Tafi, Andrea,Forli, Stefano,Botta, Bruno
experimental part, p. 4396 - 4407 (2011/07/08)
This paper deals with the design, synthesis, and evaluation of a new series of receptors for protein surface recognition. The design of these agents is based around the attachment of four constrained dipeptide chains onto a central resorc[4]arene scaffold. By varying the sequence, nature, and stereochemistry of the chains we prepared anionically functionalized N-linked peptidoresorc[4] arenes 12, 13, and 17 by Pd/C-catalyzed hydrogenation of the corresponding benzyl esters 10, 11, and 16. From this family of receptors we have identified noncompetitive inhibitors of α-chymotrypsin (ChT), which function by binding to the surface of the enzyme in the neighborhood of the active site cleft (Ki values ranging from 12.4 ± 5.1 μM for free carboxylic acid (+)-12b to 0.76 ± 0.14 μM for benzyl ester (-)-16a). For anionically functionalized receptors 12, 13, and 17 the ChT inhibition is based essentially on electrostatic interaction, and the bound enzyme can be released from the resorcarene surface by increasing the ionic strength, with its activity almost completely restored. For receptors with terminal benzyl ester groups (10 and 16) a hydrophobic network can be suggested.
HYDROLYSE ENANTIOSELECTIVE D'ESTERS D'AMINOACIDE CATALYSEE PAR L'IMIDAZOLE DANS DES MICELLES INVERSES CHIRALES.1300
Andriamanampisoa, R.,Boyer, B.,Lamity, G.,Roque, J. P.
, p. 77 - 84 (2007/10/02)
This paper reports the study of the imidazole catalyzed hydrolysis of enantiomeric pairs of three aminoacid esters in reversed micelles prepared from water, heptane and a combination of both racemic or chiral surfactants and of both racemic or chiral (S)2-octanol as cosurfactants.The enantioselectivity observed is important in the combination of chiral surfactant with racemic cosurfactant, and small in the combination of racemic surfactant with chiral cosurfactant, when ω = 20 (ω = / ).This enantioselectivity is also affected by the nature of the cosurfactant, the size of micelles and the nature of the substrate.The results prove that the reaction occurs effectively in a chiral microenvironment, the micelle membrane, and indicate that the cosurfactant is actually present in this membrane.
