E70K is a point-modified peptide or protein fragment featuring a glutamate-to-lysine substitution that alters charge distribution and electrostatic interactions. This mutation introduces a basic side chain, reshaping local hydrogen-bond patterns and structural propensity. Researchers use it to evaluate mutation-driven conformational changes and binding specificity. Applications include structure-function mapping, electrostatic surface analysis, and protein-engineering investigations.
CAT No: R2796
E70K is a peptide compound characterized by a single amino acid substitution at position 70, where glutamic acid (E) is replaced by lysine (K). This site-directed mutant peptide is widely utilized in biochemical and molecular biology research to investigate the structural and functional consequences of specific residue changes within proteins or synthetic peptides. The E70K substitution is often studied in the context of protein engineering, conformational analysis, and functional mapping, providing valuable insights into the role of charged residues in protein stability, folding, and intermolecular interactions. Its defined sequence alteration makes it a powerful tool for dissecting structure-function relationships and for modeling disease-associated protein variants in a controlled research setting.
Protein structure-function studies: Researchers employ the E70K peptide to analyze how the replacement of a negatively charged glutamic acid with a positively charged lysine influences protein conformation, stability, and dynamics. This targeted mutation enables detailed investigations into electrostatic interactions, hydrogen bonding networks, and the overall impact of residue polarity on secondary and tertiary structures. Such studies are essential for elucidating the molecular underpinnings of protein folding disorders, allosteric regulation, and the formation of functional domains.
Mutagenesis and functional assays: The E70K variant is frequently incorporated into site-directed mutagenesis experiments to assess the functional significance of the E70 position in native proteins or engineered constructs. By comparing the biochemical activity, binding affinity, or enzymatic properties of wild-type versus mutant forms, researchers can pinpoint the contribution of this specific residue to biological processes such as signal transduction, substrate recognition, or molecular assembly. These assays help clarify the mechanistic basis of protein function and inform rational design strategies for biomolecular engineering.
Peptide-protein interaction analysis: In studies focused on intermolecular recognition, the E70K peptide serves as a model system for probing the effects of charge reversal on binding interfaces. Its application in surface plasmon resonance, isothermal titration calorimetry, or co-immunoprecipitation experiments allows for quantitative evaluation of altered interaction profiles with target proteins, nucleic acids, or small molecules. Insights gained from these analyses are critical for understanding specificity determinants and for guiding the development of novel peptide-based probes or inhibitors.
Molecular modeling and computational studies: Computational chemists and structural biologists utilize the E70K sequence in in silico simulations to predict the energetic and conformational consequences of the E70K mutation. Molecular dynamics, homology modeling, and free energy calculations incorporating this mutant enable the exploration of local and global structural rearrangements, stability shifts, and potential aggregation propensities. These computational approaches complement experimental findings and provide a mechanistic framework for interpreting mutation-induced effects.
Peptide synthesis and analytical validation: The E70K peptide is also employed as a reference standard or substrate in analytical method development, such as mass spectrometry, HPLC, or capillary electrophoresis. Its defined sequence and physicochemical properties make it suitable for validating synthesis protocols, optimizing purification strategies, and calibrating analytical instrumentation. This application supports quality control and reproducibility in peptide research and manufacturing workflows, ensuring the reliability of downstream experimental results.
3. The spatiotemporal control of signalling and trafficking of the GLP-1R
4. An Open-label, Single-center, Safety and Efficacy Study of Eyelash Polygrowth Factor Serum
5. Myotropic activity of allatostatins in tenebrionid beetles
If you have any peptide synthesis requirement in mind, please do not hesitate to contact us at . We will endeavor to provide highly satisfying products and services.
Creative Peptides is a trusted CDMO partner specializing in high-quality peptide synthesis, conjugation, and manufacturing under strict cGMP compliance. With advanced technology platforms and a team of experienced scientists, we deliver tailored peptide solutions to support drug discovery, clinical development, and cosmetic innovation worldwide.
From custom peptide synthesis to complex peptide-drug conjugates, we provide flexible, end-to-end services designed to accelerate timelines and ensure regulatory excellence. Our commitment to quality, reliability, and innovation has made us a preferred partner across the pharmaceutical, biotechnology, and personal care industries.
Read More