A Structured Monodisperse PEG for the Effective Suppression of Protein Aggregation

Abstract

Teil der Lösung: Ein Polyethylenglycol (PEG) mit diskreter Dreieckstruktur wechselt bei Temperaturerhöhung von hydrophil nach hydrophob und verhindert die thermische Aggregation von Lysozym, das so nahezu 80 % seiner enzymatischen Aktivität behält. CD‐ und NMR‐spektroskopischen Studien zufolge bleiben in Gegenwart des strukturierten PEG die Lysozymstrukturen höherer Ordnung auch bei hohen Temperaturen erhalten, und nach dem Abkühlen liegt wieder die native Konformation vor.

Thermodriven Micrometer‐Scale Aqueous‐Phase Separation of Amphiphilic Oligoethylene Glycol Analogues

“…Removal of the TIPS protecting groups of 8 by tetrabutylammonium fluoride (TBAF) afforded 1 as a pale‐yellow oil. Compound 2 , with two phenyl appendages between the TEG units, was obtained by oxidative removal of the 4‐methoxybenzyl groups of an intermediate compound of triangular OEG 16. Compound 3 was prepared by the procedure reported in our previous paper 16.…”

“…Compound 2 , with two phenyl appendages between the TEG units, was obtained by oxidative removal of the 4‐methoxybenzyl groups of an intermediate compound of triangular OEG 16. Compound 3 was prepared by the procedure reported in our previous paper 16. Details of procedures and characterization data are described in the Experimental Section.…”

“…15 For example, it was known that shorter PEGs showed LCSTs at higher temperatures 14c. Recently, we developed a non‐polymeric‐structured oligoethylene glycol (OEG) analogue with a triangular structure, and reported that the geometry of the molecule affected the properties of PEG‐like molecules, such as the dehydration temperature and the protein stabilizing ability 16. Non‐polymeric triangular OEG is composed of three tetraethylene glycol (TEG) units connected with a pentaerythritol unit, the four hydroxy groups of which allow multidimensional structural diversity with minimum structural modification from the oxyethylene structure, namely, through insertion of one carbon atom.…”

Suzuki–Miyaura Coupling of Aryl Sulfonates with Arylboronic Acids Using a Morpholine–Pd(OAc)2 Catalyst System

“…Molecular structures that display subtle and controllable properties for manipulation of proteins,1 delivery of nucleic acids and other biomedical applications2 are in strong demand. Approaches to their development include the synthesis of symmetrical and higher order structures such as triangular oligoethyleneglycols,3 facial,4 rigid tandem5 and tripodal amphiphiles,6 amphiphilic nanotubes,7 gold dodecylmalonic acid‐coated nanoparticles,8 and mimicry of natural osmolytes 9. The last have been grouped10 as “methylamines” (which include, for example, trimethylamine N ‐oxide (TMAO),11 non‐detergent sulfobetaines12), polyols (including trehalose13) and amino acids.…”

Oligoethylene glycols prevent thermal aggregation of α‐chymotrypsin in a temperature‐dependent manner: Implications for design guidelines

“…[21][22][23] In fact, PEG inhibits interactions between denatured proteins, resulting in increased refolding yield 24 and prevention of thermal inactivation of proteins. 25,26 However, high molecular weight PEG is not an adequate solution additive due to its high viscosity and difficulty of removal from protein solution.…”