Beta Lactam Research Paper

In order to generate a bicyclic lactone in this experiment, a Diels-Alder adduct was produced. The bicyclic lactone to be generated was cis-1,3,3a,4,5,7a-Hexahydro-5-methyl-3-oxo-4-isobenzofuran-carboxylic Acid and was produced using a Diels-Alder reaction. The product was also analyzed quantitatively using percent yield. To prepare the Diels-Alder adduct 0.40 g of 2,4-hexadien-1-ol was added to a flask, then 5.00 mL of toluene and 0.40 g of maleic anhydride were added to the flask in that order. The mixture was warmed and stirred to induce a reaction. The reaction progress was monitored using a TLC plate with 30:70 hexane used as the mobile phase and silica gel as the stationary phase. The TLC plate revealed a new spot for the crude product, indicating the reaction had begun.

The TEM-1 type of Beta-lactamase is the most common -lactamase enzyme found in E. coli. More importantly, this enzyme is highly interactive with antibiotics by inhibiting antibiotics from accomplishing their purpose of: halting the synthesis of bacteria cell walls to cease the spread and existence of the bacteria. This makes TEM type

Gram-Negative infections are a major cause of mortality in the hospital, intensive care unit and healthcare system. For years the Carbapenems have been a major last line player in eliminating infections. Carbapenem resistance is now increasing. Two drugs Avycaz and Zerbaxa are available to fight against those microbes with Carbapenem resistance. The newly approved combination drug Avycaz is composed of Ceftazidime and Avibactam. Ceftazidime is a 3rd generation cephalosporin. It inhibits bacterial cell wall synthesis by binding to the penicillin binding protein. Avibactam is a non- Beta lactam Beta Lactamase Inhibitor. It is essential in increasing the

These mutations, no matter what process that has led to their occurrence, block the action of antibiotics by interfering with their mechanism of action (1). Currently, antibiotics attack bacteria through one of two mechanisms. In both mechanisms the antibiotic enters the microbe and interferes with production of the components needed to form new bacterial cells. Some antibiotics act on the cell membrane, causing increased permeability and leakage of cell contents. Other antibiotics interfere with protein synthesis in cells. They block one or more of the steps involved in the transformation of nucleic acids into proteins.

Two main mechanisms are responsible for resistance to aminopenicillins: enzymatic hydrolysis of the antibiotic and a change in penicillin-binding proteins (PBPs). The more frequent is the production of β-lactamase, usually of the TEM-1 type but sometimes of the ROB-1 type [2]. The incidence of strains producing β-lactamase is particularly high in many countries [3;

As we seen in the mechanism of action all beta-lactam antibiotics, share a basic chemical structure that includes a three carbon, one nitrogen cyclic amine structure is known as the beta-lactam ring. Beta-lactam ring attached with a side chain having a variable group to the core structure of by a peptide bond. The variation of the side chain contributes to antibacterial activity.FDA has approved over 34 beta-lactam compounds as active ingredients in drugs for human use. Beta-lactam antibiotics have the following five classes:

Upon search it was found that the most common side effects presented with lacosamide were headache, dizziness, nausea, rashes and double vision and it causes serious side effects upon receiving large dose ranging from 200-400 mg/day. Suicidal thought, Psychiatric disorders, sinus node dysfunction and hyper activity have been reported in patients receiving lacosamide.

A continual production of lactic acid through fermentation may result in an increase of acidity within muscle cells and blood.

β-lactam antibiotics (beta-lactam antibiotics) are a class of broad-spectrum antibiotics that contain a beta-lactam ring in their molecular structures. Most β-lactam antibiotics act by inhibiting cell wall biosynthesis.

Bacterial cells eukaryotes have a cell wall that provides protection to the bacterial cells. Targeting of the cell wall would result in interruption of bacterial cell structure which would result in an osmotic imbalance resulting into cell

Beta-secretase enzyme (BACE), one of the key enzyme, acting as a drug target, has become a major concern for development of inhibitors. Inhibitors that can reduce beta amyloids in the neurons has become slow due to incomplete understanding the function and regulation of enzyme in brain. The penetration of the drug across brain can block the catalytic pocket of the enzyme [11, 12]. BACE-1, a 501 long amino acid, type-1 transmembrane aspartic protease, localized in the Golgi apparatus and late endosomes [13]. It has been also reported the localization of bace-1 is in the trans-Golgi complex and endosome and can be reinternalized back to endosomes from the cell surface [14, 15]. BACE-1 undergoes glycosylation on 4 residues of Asn and acetylation

Enzymes are the very successful machines of natural life. They are in charge of lowering so as to catalyze responses the enactment vitality for these responses. Enzymes are comprised of proteins interpreted from nucleic corrosive coding material, so they have particular duties inside of a life form. Beta-lactamase is a enzyme that separates beta-lactam anti-toxins like penicillin. In this lab, the viability of the beta-lactamase catalyst was tried at diverse temperatures. The beginning speculation of the trial was that enzymatic action would increment as temperature expanded, in spite of the fact that at 60 degrees Celsius the chemical would denature. This was somewhat reflected in the information. The chemical did denature at 60 degrees; in

Carbapenems are a class of beta-lactam antibiotics that are effective against many gram-positive, gram-negative, aerobic and anaerobic microorganisms (Holten and Onusko, 2000). Beta-lactam is a key component to the core structure of carbapenem which consists of 2-Azetidinone where two hydrogen atoms are substituted for two variable R groups (see Figure 1).

Ceftazidime is a third generation cephalosporin antibiotic used to treat a number of bacterial infections, particularly Pseudomonas and other Gram negatives, and its activity relies on binding of essential penicillin-binding proteins (PBPs) (1). Despite its effectiveness against certain bacteria, there have been reports of rapidly increasing incidences of antibacterial resistance to ceftazidime caused by extended-spectrum β-lactamase (ESBL)-producing Enterobacteriaceae (2). Recently, a new beta-lactam/beta-lactamase inhibitor combination, ceftazidime-avibactam (AVYCAZ) has shown to have “in vitro activity against Enterobacteriaceae in the presence of some beta-lactamases and extended-spectrum beta-lactamases” and is FDA-approved for treating complicated intra-abdominal infections as well as complicated urinary tract infections (1). Due to the resistance frequency of inpatient Enterobacteriaceae isolates at the University of Washington Medical Center (4), susceptibility testing of Ceftazidime and Ceftazidime-Avibactam are crucial to ensure antibiotic treatment efficacy and to take action to reduce the spread of multi-drug resistant bacteria in a hospital setting.

Illnesses caused by disease and other infections have troubled inhabitants of this world for centuries. However, modern science and epidemiology allow us to break down the organisms that cause the illness in order to treat and prevent it. We can now understand the classification and type of organism as well as its life cycle. We can discover its mode of transmission and methods to diagnose it. By determining these factors, the future of the organism can be determined and lives can be saved. Today, many new diseases are being examined in hopes of containing ailments and treating those who have contracted them. One such ailment is an organism called New Delhi Metallo-beta-lactamase, more