GE 2270A, a groundbreaking biomedicine, emerges as a remarkable anticancer therapeutic agent evoking profound intrigue in scientific circles. Its unyielding focus on targeted cancer cell suppression manifests as an inhibitory force confounding their proliferation, thereby engendering a noteworthy hindrance against oncogenic dissemination. Boasting remarkable efficacy demonstrated through meticulous clinical evaluations, this formidable pharmaceutical entity stands resolute as an efficacious modality for eradicating the scourge of cancer.
CAT No: R2076
CAS No:134861-34-0
Chemical Name:(2S)-1-[(4S)-2-[2-[(18S,25S,35S)-35-[(S)-hydroxy(phenyl)methyl]-28-(methoxymethyl)-21-methyl-18-[2-(methylamino)-2-oxoethyl]-16,23,30,33-tetraoxo-25-propan-2-yl-3,13,20,27,37-pentathia-7,17,24,31,34,39,40,41,42,43-decazaheptacyclo[34.2.1.12,5.112,15.119,22.126,29.06,11]tritetraconta-1(38),2(43),4,6(11),7,9,12(42),14,19(41),21,26(40),28,36(39)-tridecaen-8-yl]-1,3-thiazol-4-yl]-4,5-dihydro-1,3-oxazole-4-carbonyl]pyrrolidine-2-carboxamide
GE 2270A is a cyclic depsipeptide antibiotic produced by fermentation of Planobispora rosea, distinguished by its unique structure that combines both peptide and ester bonds. As a member of the thiopeptide class, GE 2270A exhibits potent activity against Gram-positive bacteria due to its ability to inhibit protein synthesis via binding to elongation factor Tu (EF-Tu). Its complex macrocyclic framework and defined mode of action have made it a subject of significant interest in biochemical research, especially in studies of ribosomal function and the development of novel antimicrobial agents. The compound's intricate architecture and mechanism provide a valuable model for exploring peptide-based inhibition and structure-activity relationships within the thiopeptide family.
Antibiotic mechanism of action studies: GE 2270A serves as a critical tool for elucidating the molecular mechanisms underlying thiopeptide antibiotic activity. By targeting the elongation factor Tu, it disrupts the protein synthesis process in susceptible bacterial strains. Researchers utilize this molecule to investigate the structural basis of EF-Tu inhibition, which aids in understanding how bacterial translation can be selectively targeted and informs the rational design of next-generation antibiotics with improved specificity and reduced resistance potential.
Structure-activity relationship (SAR) research: The unique macrocyclic structure of GE 2270A, featuring both peptide and ester linkages, makes it an exemplary scaffold for SAR studies. Chemists and biochemists employ it to systematically modify functional groups and assess the impact on biological activity. Such investigations provide insight into the essential chemical features required for potent EF-Tu inhibition and help define the pharmacophore responsible for antimicrobial efficacy, thus guiding synthetic efforts toward optimized thiopeptide analogs.
Peptide biosynthesis and enzymology: As a representative of nonribosomal peptide synthetase (NRPS)-derived compounds, GE 2270A is frequently used in studies of peptide biosynthetic pathways. Its production involves intricate enzymatic steps, including cyclization and esterification, making it a model substrate for dissecting NRPS machinery. Researchers leverage it to probe the specificity, mechanism, and engineering potential of biosynthetic enzymes, contributing to advances in combinatorial biosynthesis and the generation of novel peptide-based molecules.
Analytical method development: The structural complexity and defined biological activity of GE 2270A make it a valuable reference standard in analytical chemistry. Laboratories use it to validate and calibrate chromatographic and spectrometric techniques for the detection and quantification of thiopeptide antibiotics. Its application in method development ensures accurate measurement of similar compounds in fermentation broths, biological samples, or environmental matrices, supporting both quality control and research workflows.
Antimicrobial resistance research: The well-characterized interaction between GE 2270A and bacterial EF-Tu provides a platform for investigating mechanisms of resistance to thiopeptide antibiotics. Scientists employ it to select and characterize resistant bacterial mutants, study compensatory mutations in target proteins, and evaluate the efficacy of combination therapies. These applications deepen understanding of resistance evolution and inform strategies to counteract or circumvent antimicrobial resistance in pathogenic bacteria.
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