Native Proteomics

Native proteomics involves the systematic analysis and study of proteins without altering their three-dimensional structure. This approach is applicable not only to individual protein studies but also to the analysis of protein networks and inter-protein interactions. Proteins typically perform cellular functions by forming complexes with other proteins or molecules, and many biological processes, including signal transduction, gene expression regulation, and cell cycle control, depend on precise protein coordination. Native proteomics, by preserving these interactions, can elucidate the interconnections and dynamic changes of proteins within cells. This method is pivotal for understanding cellular functions, investigating disease mechanisms, and exploring novel drug targets. Beyond basic protein analysis, it sheds light on the structural characteristics of proteins. The folding state, substructure, and interaction with other molecules directly influence protein activity. By maintaining proteins in their native conformations, native proteomics provides insights into protein function, especially for multi-subunit complexes or large protein networks that cannot be effectively analyzed under denatured conditions. Another application of native proteomics is in drug screening and design. While traditional drug screening focuses on small molecules binding to target proteins, many drugs' mechanisms and therapeutic effects rely on proteins' natural characteristics and functions. This technology enables researchers to evaluate drugs' effects on proteins more accurately, including changes in protein structure, modifications, and interactions, thus optimizing drug development.

 

Native proteomics typically uses advanced mass spectrometry techniques along with low-temperature or suitable chemical conditions to prevent protein denaturation during analysis. This approach significantly reduces biases from conformational changes, providing a more accurate reflection of proteins' natural states. In proteomics research, many protein functions and activities are closely linked to their spatial structure, and denaturation may impact their biological effects. Native proteomics, by maintaining proteins' native conformations, can reveal complex biological phenomena such as protein folding, the role of molecular chaperones, and protein-target interactions.

 

Compared to traditional proteomic methods, native proteomics offers a significant advantage in studying post-translational modifications (such as phosphorylation, acetylation, glycosylation). These modifications are crucial for protein function regulation and are often influenced by spatial structure and environmental conditions, accurately captured only when proteins maintain their native conformation. Consequently, this proteomic technology holds significant potential in disease research, drug development, and biomarker discovery.

 

In practice, the challenges of native proteomics mainly arise from sample complexity and technical demands. Samples typically originate from complex biological systems (like cells, tissues, blood) containing thousands of proteins, each potentially exhibiting diverse conformations and functions under different conditions. Hence, extracting and stabilizing proteins' native states in complex backgrounds is a key technical challenge. To address this, native proteomics often integrates advanced separation technologies (like ultra-high-performance liquid chromatography) with high-sensitivity mass spectrometry to ensure efficient, accurate analysis of target proteins and their modifications.

 

MtoZ Biolabs offers high-quality proteomics analysis services, aiding clients in deeply analyzing critical biological information, such as protein expression levels, modification states, and interactions, while preserving proteins' natural structures.

 

MtoZ Biolabs, an integrated chromatography and mass spectrometry (MS) services provider.