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This article will discuss novel analytical methods for the discovery and trace analysis of biochemically active compounds in three main areas: protein analysis, screening technologies and multidimensional separations. The research in protein analysis describes analytical methods that involve automation and integration of sample clean-up, followed by separation and detection of the peptides/proteins. [ABSTRACT FROM AUTHOR]

A novel tandem mass spectrometry instrument (PTM Discovery System™) offers the application of two different MS fragmentation techniques (i.e. collisionally induced dissociation, CID, and electron transfer dissociation, ETD) showing highly complementary fragmentation results. The information obtained from both techniques is ideally suited for the characterization of post translational modifications (PTM), such as phopshorylation. ETD based fragmentation shows a similar short duty cycle as common CID allowing fast peptide identification and characterization in combination with online separation techniques. [ABSTRACT FROM AUTHOR]

The article focuses on the impact of the size of pore packing materials for peptide separations in ultra performance liquid chromatography peptide mapping. The pore size materials of 130 A and 300 A are compared in the separation of its two complex peptide digests. The result shows that both peptide separation technology columns give useful separations of peptides over a wide range of sizes and chemical properties.

Crude synthetic peptide samples were separated on preparative Atlantis™ dc18 columns. Fraction collection was triggered by the mass-to-charge (rn/z) ratio of the peptides. which specified the target peptide in the collected fraction to increase the fraction purities. Mass-directed peptide purification was more robust than UV-based collection under overloading conditions, and increased the traction purities. LC-MS-MS analysis was further employed to identify the impurities in the crude synthetic peptide sample. This study demonstrates high mass loading, selective purification. high recoveries and purity, and the capability of utilizing mass-directed fractionation for purifying peptides on preparative RPLC columns. [ABSTRACT FROM AUTHOR]

Discusses the separation of peptides by hydrophilic interaction chromatography using the TSKgel Amide-80 column, a method developed by Tosoh Bioscience GmbH that provides excellent selectivity for separating peptides in hydrophilic interaction chromatography. Overview of methods for the separation of peptides with many acidic and basic residues; Effect of acetonitrile concentration on peptide retention.

Discusses the direct separation of chiral amino acids, hydroxy acids, and dipeptides by ligand exchange. Description of Chirex ligand exchange phase 3126; Instrumentation and equipment; Control of analyte retention times.

Discusses the use of three-micrometer polymeric particles for the high resolution/fast reversed phase-high performance liquid chromatographic analysis of synthetic peptides. Characteristics of the polymeric particle; Experimental conditions; Separation of peptide standards; Potential applications of the analytical method.