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Updated: Jun 4, 2026

A Tailored HPLC Purification Protocol That Yields High-purity Amyloid Beta 42 and Amyloid Beta 40 Peptides, Capable of Oligomer Formation
Published on: March 27, 2017
Hexylacrylate-based mixed-mode monolith, a stationary phase for the nano-HPLC separation of structurally related
Ayat Abbood1, Christine Herrenknecht, Gaëlle Proczek
1Univ. Paris-Sud, UMR CNRS 8612, LPNSS, Faculté de Pharmacie, 92296 Châtenay-Malabry, France.
Abstract:
The potential of an in situ photopolymerized hexylacrylate-based monolithic stationary phase-bearing sulfonic acid groups was investigated by studying the chromatographic retention of small structurally related peptides (enkephalins) by nano-LC. Several retention mechanisms were highlighted. First, a reverse-phase chromatographic behavior toward neutral solutes due to hexylacrylate-moieties was demonstrated. Second, an evaluation of the influences of buffer pH suggested the involvement of a cation-exchange mechanism due to the presence of 2-acrylamido-2-methyl-1-propanesulfonic acid. This cation-exchange phenomenon was confirmed by the clear influence of Na(+) concentration in the mobile phase on peptide retention.
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