Covalent immobilization: A review from an enzyme perspective

Chemical Engineering Journal, Journal Year: 2024, Volume and Issue: unknown, P. 158054 - 158054

Published: Nov. 1, 2024

Language: Английский

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Affinity Electrophoresis of Proteins for Determination of Ligand Affinity and Exploration of Binding Sites

International Journal of Molecular Sciences, Journal Year: 2025, Volume and Issue: 26(7), P. 3409 - 3409

Published: April 5, 2025

Affinity gel electrophoresis was introduced about 50 years ago. Proteins interact with a ligand immobilized in the support. Specific interactions cause decrease electrophoretic mobility. The presence of free ligand, competing an restores In affinity capillary electrophoresis, is mobile, and its interaction specific protein changes mobility protein-ligand complex. This review mostly focuses on electrophoresis. theoretical basis this technique, immobilization strategies, principles for determination are addressed. Factors affecting specificity strength discussed, particular, structure matrix, pH, temperature, hydrostatic pressure, solvent, co-solvents, electric field, other physico-chemical conditions. Capillary uses also briefly introduced. can be used qualitative quantitative purposes. includes detection proteins complex media, investigation interactions, heterogeneity, molecular genetic polymorphism, estimation dissociation constants complexes, conformational stability binding sites. Future prospects, particular screening engineered mutants potential new drugs, coupling to analytical methods, ultra-microtechnological developments, addressed light trends renewal old technique.

Language: Английский

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The cryoprotective effect of Litopenaeus vannamei head-derived peptides and its ice-binding mechanism.

Current Research in Food Science, Journal Year: 2024, Volume and Issue: 9, P. 100886 - 100886

Published: Jan. 1, 2024

Language: Английский

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Enzymes and Natural Products

Published: Jan. 1, 2025

Language: Английский

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A simplified optimization approach for sample preparation workflow in LC‐MS‐based quantitative proteomic analysis: Biological samples to peptides

Archiv der Pharmazie, Journal Year: 2025, Volume and Issue: 358(3)

Published: March 1, 2025

Quantitative proteomics, an integral subfield within is pivotal for elucidating complex biological processes. By integrating with other omics data, quantitative proteomics facilitates system-level analysis and significantly advances our understanding of cellular networks disease mechanisms. The ongoing advancements in technology boost its importance by improving analytical accuracy. This review focuses on employing liquid chromatography-mass spectrometry (LC-MS), a cornerstone technique renowned sensitivity, selectivity, accuracy, throughput. efficacy LC-MS heavily reliant sample preparation, which encompasses protein extraction, total estimation, reduction, alkylation, digestion, cleanup. For the very first time, this article provides detailed examination preparation methods offering insights guidelines that researchers can utilize to refine their experimental protocols were not critically evaluated before. optimizing workflows, enhance robustness reproducibility proteomic studies. complexities optimize workflow improve results. comprehensive overview strategies using LC-MS, discussing underlying principles key considerations each step. delving into aims aid workflows achieve robust reproducible results, ultimately drive innovations breakthroughs biomedical research healthcare.

Language: Английский

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Generic insights into the softening-related biopolymer changes during cooking of common bean (Phaseolus vulgaris L.) accessions of different market classes

Journal of Food Engineering, Journal Year: 2025, Volume and Issue: unknown, P. 112571 - 112571

Published: March 1, 2025

Language: Английский

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Gel Electrophoresis in Protein and Peptide Analysis: History and Current Status

Encyclopedia of Analytical Chemistry, Journal Year: 2025, Volume and Issue: unknown, P. 1 - 23

Published: March 27, 2025

Abstract Gel electrophoresis is a widely used method in biochemical research; number of different forms gel have been developed and applied to the analysis proteins peptides. The most popular form polyacrylamide (PAGE), which are separated within matrix on basis differences their charge density and/or relative molecular mass ( M r ). Polyacrylamide also as media for generation pH gradients an isoelectrofocusing (IEF) technique, where separation due isoelectric point (pI). Two‐dimensional (2D) extremely powerful combining pI (in IEF) sodium dodecyl sulfate PAGE (SDS‐PAGE)). Agarose gels rarely today electrophoretic proteins; utility mainly restricted immunoelectrophoretic techniques, allow characterization by migration immunological properties. This article provides brief history describes principles major techniques. fields research demonstrated. Topics included analytical small‐scale preparative separations complex samples; determination electrophoretically polypeptides; micropreparation protein sample its further immunochemical, enzymatic proteomic analysis; study interactions with ligands; examination unfolding quaternary structure. advantages limitations described techniques discussed.

Language: Английский

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Effects of Temperature and Salt Stress on Cereus fernambucensis Seed Germination

Biology, Journal Year: 2025, Volume and Issue: 14(4), P. 393 - 393

Published: April 9, 2025

The Brazilian Atlantic Forest is recognized as a biodiversity hotspot with high levels of Cactaceae endemism, attracting significant attention for conservation efforts [...]

Language: Английский

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Osmolyte induced protein stabilization: modulation of associated water dynamics might be a key factor

Physical Chemistry Chemical Physics, Journal Year: 2023, Volume and Issue: 25(47), P. 32602 - 32612

Published: Jan. 1, 2023

The mechanism of protein stabilization by osmolytes remains one the most important and long-standing puzzles. traditional explanation osmolyte-induced stability through preferential exclusion from surface has been seriously challenged observations like concentration-dependent reversal stabilization/destabilization. more modern stabilization/destabilization considers an indirect effect due to distortion water structure. It provides a general mechanism, but there are numerous examples protein-specific effects, i.e., particular osmolyte might stabilize protein, destabilize other, that could not be rationalized such explanation. Herein, we hypothesized modulation associated critical factor in controlling medium. Taking different papain as proved our proposal explain media. Stabilizing rigidify structures around whereas destabilizing make them flexible. strong correlation between dynamics, fact dynamics very much specific, established importance considering explaining proteins. More interestingly, took another bromelain, for which traditionally stabilizing osmolyte, sucrose, acts stabilizer at higher concentrations destabilizer lower concentrations. Our successfully explains observations, is probably impossible any known mechanisms. We believe this report will trigger research area.

Language: Английский

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Buffalo worm (Alphitobius diaperinus) proteins: Structural properties, proteomics and nutritional benefits

Food Chemistry, Journal Year: 2024, Volume and Issue: 464, P. 141757 - 141757

Published: Oct. 22, 2024

Biophysical methods such as circular dichroism (CD) and differential scanning calorimetry (DSC) have been minimally used to characterize insect-derived proteins. This study examines the insect Alphitobius diaperinus a potential protein source. Techniques alkaline solubilization coupled isoelectric precipitation Osborne fractionation were obtain concentrates fractions (albumins, globulins, prolamins, glutelins). SDS-PAGE results showed dominant bands at 78.3, 73.3, 49.3, 34.5, 32.0, 10.3 kDa. All had over 60 % α-helix β-sheet structures, indicating stable conformations. Prolamins high surface hydrophobicity thermal stability. Nutritionally, glutelins exhibited highest concentration of essential amino acids (68.75 g/100 g protein), demonstrated superior In vitro protein-digestibility (84.04 %) well corrected acid score (73.11 %). Therefore, this characterized structural-function relationship A. proteins collectively assessed their suitability safety for human consumption.

Language: Английский

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