Taiy Chemical
Ac-Lys(Ac)-D-Ala-D-lactic Acid
Synonym N/A
Species N/A
Protein Accession N/A
Purity Greater than 95%
Endotoxin Level Less than 1EU/ug
Biological Activity N/A
Expression System Chemical synthesis
Fusion Tag N/A
Predicted Molecular Mass 556.58 Da
Formulation Supplied as a lyophilized powder
Reconstitution Centrifuge vial before opening. Reconstitute in sterile ddH2O to a concentration of 1 mg/ml
Storage & Stability Store at -20°C upon receipt. Aliquot and store at -20°C to -80°C. Avoid repeated freeze-thaw cycles.
FAQ
What is the chemical structure and function of Ac-Lys(Ac)-D-Ala-D-lactic acid?

Ac-Lys(Ac)-D-Ala-D-lactic acid is a specialized peptide compound characterized by the presence of a unique sequence involving acetylated lysine, D-alanine, and D-lactic acid. The acetylation of the lysine residue is a post-translational modification that plays a significant role in various biological functions, often influencing protein-protein interactions, stability, and cellular localization. In the context of peptide chemistry, the acetylation can affect the compound’s solubility and resistance to enzymatic degradation. This specific peptide sequence can be important in research contexts where the study of cell wall biosynthesis and antibiotic resistance mechanisms, especially in bacterial organisms, is relevant. D-alanine and D-lactic acid residues are unusual in mammalian biology but are often components of bacterial cell wall peptidoglycan - a critical factor in the structure and integrity of bacterial cells. The inclusion of D-lactic acid instead of the typical D-alanine in the cell wall precursor is a well-known mechanism of resistance towards certain antibiotics like vancomycin in some pathogenic bacteria. By studying compounds like Ac-Lys(Ac)-D-Ala-D-lactic acid, researchers can gain insights into how bacterial systems modify their cell wall structure and composition to evade antibiotic action. This further underscores the importance of understanding such compounds for developing strategies to counteract antibiotic resistance and developing novel therapeutic agents. Additionally, in laboratory settings, Ac-Lys(Ac)-D-Ala-D-lactic acid could be used as a standard or a reference for peptide synthesizing and modification techniques, evaluating how these modifications impact the overall behavior of peptide-based systems. Researchers focusing on drug development, diagnostics, and understanding complex biological systems may utilize this compound in various assays and experimental designs to unravel new insights related to microbial physiology and biochemistry.

How does Ac-Lys(Ac)-D-Ala-D-lactic acid fit into research on antibiotic resistance?

Ac-Lys(Ac)-D-Ala-D-lactic acid is integral to understanding antibiotic resistance, particularly how bacteria resist treatment by modifying cell wall synthesis pathways. This compound's structure mimics a known resistance mechanism that involves the alteration of the terminal residues in peptidoglycan precursors of bacterial cell walls, specifically substituting D-alanine-D-alanine dipeptides with D-alanine-D-lactic acid or similar analogs. Such modifications are pivotal to the resistance exhibited by certain bacterial strains against glycopeptide antibiotics like vancomycin, which function by binding to the D-alanine-D-alanine termini of nascent peptidoglycan chains and inhibiting cell wall synthesis. By incorporating D-lactic acid instead of the second D-alanine, bacteria reduce the binding affinity of these antibiotics due to the steric and chemical nature of the modification, allowing peptidoglycan polymerization to proceed unimpaired and leading to antibiotic resistance. Research utilizing Ac-Lys(Ac)-D-Ala-D-lactic acid might focus on deciphering these alterations' structural and functional roles at a molecular level. By studying these changes, scientists can gain insights into how resistance is conferred, which is crucial for the development of next-generation antibiotics capable of circumventing these bacterial defense mechanisms. Moreover, this compound can be used in designing in vitro models of bacterial cell wall synthesis and degradation, providing a controlled environment for studying the efficacy of novel antibacterial agents. Additionally, it can serve as a template or scaffold for developing inhibitors that target modified bacterial enzymes responsible for these resistance pathways. Identifying and characterizing such inhibitors could form the basis of new therapeutic strategies that tackle hard-to-treat infections caused by resistant bacterial species. Overall, Ac-Lys(Ac)-D-Ala-D-lactic acid plays a vital role in antibiotic resistance research by providing a tool to study and counteract bacterial adaptability and survival in the face of antibiotic interventions.

In what ways is Ac-Lys(Ac)-D-Ala-D-lactic acid important for studies in bacterial cell wall synthesis?

Ac-Lys(Ac)-D-Ala-D-lactic acid holds substantial importance in studies focused on bacterial cell wall synthesis due to its role in mimicking natural modifications found in bacterial peptidoglycan layers. The bacterial cell wall is composed of a mesh-like structure primarily made of peptidoglycan, which provides mechanical strength and protection for bacterial cells. Understanding this structure is critical for insights into how bacteria grow, divide, and maintain integrity. In some bacteria, altered peptidoglycan precursors incorporating D-lactic acid in place of D-alanine are key adaptations to evade action by certain antibiotics such as vancomycin. Therefore, Ac-Lys(Ac)-D-Ala-D-lactic acid allows researchers to investigate how these modifications affect the construction and functionality of the bacterial cell wall. The presence of acetylated lysine also adds a level of complexity, providing insight into how additional post-translational modifications might influence protein interactions or the stability of wall-associated enzymes and components. Insights gained from such studies can elucidate fundamental processes of bacterial cell physiology and may help unravel processes limiting cell growth or survival under antibiotic pressure. Researchers can employ this compound in designing assays and experiments to test cell wall synthesis enzymes, critical for developing inhibitors that could halt bacterial growth by disrupting this essential process. Furthermore, Ac-Lys(Ac)-D-Ala-D-lactic acid can help identify specific genes and proteins involved in resistance pathways, providing comprehensive knowledge about molecular pathways important in bacterial adaptation and survival. Such findings could direct the future development of therapeutic strategies that target bacterial cell walls with refined specificity and efficacy. Overall, Ac-Lys(Ac)-D-Ala-D-lactic acid provides a crucial tool for comprehending the nuances of bacterial cell wall architecture and synthesis, essential for developing novel antibacterial strategies and understanding bacterial pathogenesis and resistance development.

Can Ac-Lys(Ac)-D-Ala-D-lactic acid be used in novel therapeutic development?

Ac-Lys(Ac)-D-Ala-D-lactic acid has significant potential in the development of new therapeutic agents, particularly those targeting resistant bacterial infections. This potential arises from its structure, which resembles modifications associated with antibiotic resistance in some bacteria, making it an excellent tool for understanding and addressing this issue. By utilizing this compound in research, it becomes possible to explore how bacterial pathogens alter their cell wall components to evade antibiotics. Understanding these mechanisms can guide the design of new drugs that can either prevent these modifications or work effectively against bacteria despite them. For example, investigating how Ac-Lys(Ac)-D-Ala-D-lactic acid interacts with bacterial enzymes responsible for peptidoglycan synthesis can offer insights into novel targets for antimicrobial therapy. Furthermore, it helps in screening small molecule inhibitors or peptides that can disrupt these modified peptidoglycan chains, effectively rendering bacteria susceptible to standard treatments again. This peptide might also open avenues for developing novel vaccine adjuvants, focusing on educating the immune system to recognize these modified peptide structures, potentially boosting the immune response against antibiotic-resistant bacteria. By studying and manipulating this structure, researchers can even engineer enzymes or antibodies with specificity for bacterial structures bearing this and similar modifications, contributing to treatment options that are not reliant solely on traditional antibiotics. Beyond direct antimicrobial development, this compound can impact new diagnostic tools to identify resistant strains quickly and accurately, essential for timely and effective treatment decisions. Thus, Ac-Lys(Ac)-D-Ala-D-lactic acid serves not only as a critical research tool but also as a springboard for innovative therapies and diagnostic techniques that address one of the modern world’s most pressing health challenges: antibiotic resistance.

What research techniques commonly involve Ac-Lys(Ac)-D-Ala-D-lactic acid?

Research involving Ac-Lys(Ac)-D-Ala-D-lactic acid often incorporates cutting-edge techniques in molecular biology, biochemistry, and microbiology to elucidate the subtleties of bacterial resistance and metabolism. Given its role in mimicking bacterial peptidoglycan modifications, this compound is frequently used in structural biology studies employing X-ray crystallography or nuclear magnetic resonance (NMR) spectroscopy to understand protein-ligand interactions at an atomic level. These techniques help capture the exact binding interactions between Ac-Lys(Ac)-D-Ala-D-lactic acid and bacterial enzymes, offering insights into the biological pathways influenced by these modifications. Additionally, mass spectrometry could be utilized to analyze the presence and abundance of these modified peptides within bacterial cultures, providing data on how their levels fluctuate during different growth phases or under antibiotic stress. Moreover, in a cellular context, fluorescence microscopy or other imaging modalities might be leveraged to observe the spatial dynamics of these peptides across bacterial populations. Bioinformatics tools and molecular dynamic simulations may be employed to model these interactions and predict how novel inhibitors or drugs could alter the binding landscape, providing predictions before proceeding with expensive and time-consuming wet-lab experiments. Polymerase chain reaction (PCR) and advanced genomic techniques, such as CRISPR and RNA sequencing, can help ascertain how genes associated with the processing of these modified peptides are regulated, providing a genetic roadmap for targeting bacterial resistance mechanisms. Using these robust and multifaceted research methods, scientists can produce holistic insights into how bacteria adapt structurally and functionally to pressures such as antibiotic treatments and environmental stressors, ultimately supporting the development of novel therapeutics and diagnostic tools. Overall, the diverse range of research techniques involving Ac-Lys(Ac)-D-Ala-D-lactic acid underscores the compound's versatility and importance in advancing the understanding of bacterial physiology and resistance mechanisms.
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