Hydrophobic Interaction Chromatography for Bottom-Up Proteomics Analysis of Single Proteins and Protein Complexes

Rackiewicz, Michal; Grosse‐Hovest, Ludger; Alpert, Andrew J.; Zarei, Mostafa; Dengjel, Jörn

doi:10.1021/acs.jproteome.7b00015

Cited by 6 publications

(2 citation statements)

References 29 publications

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“…Hydrophobic interaction chromatography (HIC) has emerged as a crucial bioanalytical technology for the comprehensive characterization of individual proteins ( O’Connor and Cummins, 2017 ). It is a high-resolution chromatography method that operates by weakly interacting hydrophobic ligands on the stationary phase with hydrophobic regions on the surface of proteins’ tertiary structure ( Rackiewicz et al, 2017 ). In HIC, solutes (proteins) are adsorbed and isolated on a stationary solid phase (a two-dimensional system) consisting of immobilized hydrophobic groups ( Jennissen, 2001 ).…”

Section: Purification Of Protein Hydrolysatementioning

confidence: 99%

Protein Hydrolysate from Underutilized Legumes: Unleashing the Potential for Future Functional Foods

Azman,

Mohd Isa,

Mohd Zin

et al. 2023

Prev. Nutr. Food Sci.

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Proteins play a vital role in human development, growth, and overall health. Traditionally, animal-derived proteins were considered the primary source of dietary protein. However, in recent years, there has been a remarkable shift in dietary consumption patterns, with a growing preference for plant-based protein sources. This shift has resulted in a significant increase in the production of plant proteins in the food sector. Consequently, there has been a surge in research exploring various plant sources, particularly wild, and underutilized legumes such as Canavalia , Psophocarpus , Cajanus , Lablab , Phaseolus , and Vigna , due to their exceptional nutraceutical value. This review presents the latest insights into innovative approaches used to extract proteins from underutilized legumes. Furthermore, it highlights the purification of protein hydrolysate using Fast Protein Liquid Chromatography. This review also covers the characterization of purified peptides, including their molecular weight, amino acid composition, and the creation of three-dimensional models based on amino acid sequences. The potential of underutilized legume protein hydrolysates as functional ingredients in the food industry is a key focus of this review. By incorporating these protein sources into food production, we can foster sustainable and healthy practices while minimizing environmental impact. The investigation of underutilized legumes offers exciting possibilities for future research and development in this area, further enhancing the utilization of plant-based protein sources.

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Section: Purification Of Protein Hydrolysatementioning

confidence: 99%

Protein Hydrolysate from Underutilized Legumes: Unleashing the Potential for Future Functional Foods

Azman,

Mohd Isa,

Mohd Zin

et al. 2023

Prev. Nutr. Food Sci.

View full text Add to dashboard Cite

show abstract

“…However, the presence of salt in the IEX mobile phases may disrupt native PPIs [81]. Conversely, high salt content is used to enhance the adsorption of hydrophobic protein surfaces to the solid support in HIC, and complexes are eluted upon decreasing salt gradient [82]. Apart from soluble complexes, it has been demonstrated that with mild or non-denaturing detergents, it is possible to co-fractionate membrane-bound complexes, for instance, the mitochondrial membrane-bound complexes using BN-PAGE [83,84].…”

Section: Co-fractionation Coupled To Mass Spectrometry (Cofrac-ms)mentioning

confidence: 99%

Recent progress in mass spectrometry-based strategies for elucidating protein–protein interactions

Low

Syafruddin

Mohtar

et al. 2021

Cell. Mol. Life Sci.

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Protein-protein interactions are fundamental to various aspects of cell biology with many protein complexes participating in numerous fundamental biological processes such as transcription, translation and cell cycle. MS-based proteomics techniques are routinely applied for characterising the interactome, such as affinity purification coupled to mass spectrometry that has been used to selectively enrich and identify interacting partners of a bait protein. In recent years, many orthogonal MS-based techniques and approaches have surfaced including proximity-dependent labelling of neighbouring proteins, chemical cross-linking of two interacting proteins, as well as inferring PPIs from the co-behaviour of proteins such as the co-fractionating profiles and the thermal solubility profiles of proteins. This review discusses the underlying principles, advantages, limitations and experimental considerations of these emerging techniques. In addition, a brief account on how MS-based techniques are used to investigate the structural and functional properties of protein complexes, including their topology, stoichiometry, copy number and dynamics, are discussed. Keywords Affinity purification coupled to mass spectrometry (AP-MS) • Proximity-dependent biotinylation coupled to MS (PDB-MS) • Cross-linking mass spectrometry (XL-MS) • Co-fractionation mass spectrometry (coFrac-MS) • Thermal proximity coaggregation (TPCA)

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Effects of the Extracellular Matrix on the Proteome of Primary Skin Fibroblasts

Tölle

Dengjel

2019

Methods in Molecular Biology

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Hydrophobic Interaction Chromatography for Bottom-Up Proteomics Analysis of Single Proteins and Protein Complexes

Cited by 6 publications

References 29 publications

Protein Hydrolysate from Underutilized Legumes: Unleashing the Potential for Future Functional Foods

Protein Hydrolysate from Underutilized Legumes: Unleashing the Potential for Future Functional Foods

Recent progress in mass spectrometry-based strategies for elucidating protein–protein interactions

Effects of the Extracellular Matrix on the Proteome of Primary Skin Fibroblasts

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