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.