CDNF is a secreted neurotrophic factor that contains 8 conserved cysteine residues, much like its relative MANF. CDNF and its structural homolog MANF each contain an N-terminal saposin-like lipid binding domain and a carboxyl-terminal domain, which is not homologous to previously characterized protein structures. CDNF is expressed in several tissues, including the embryonic and postnatal brains of mice, as well as the heart, skeletal muscle, and testis. It has been shown to promote survival, growth and function of dopamine specific neurons. CDNF and MANF can prevent 6-OHDA induced degeneration of dopaminergic neurons by triggering survival pathways in a rat experimental model of Parkinson disease.

CDNF is a secreted neurotrophic factor that contains 8 conserved cysteine residues, much like its relative MANF. CDNF and its structural homolog MANF each contain an N-terminal saposin-like lipid binding domain and a carboxyl-terminal domain, which is not homologous to previously characterized protein structures. CDNF is expressed in several tissues, including the embryonic and postnatal brains of mice, as well as the heart, skeletal muscle, and testis. It has been shown to promote survival, growth and function of dopamine specific neurons. CDNF and MANF can prevent 6-OHDA induced degeneration of dopaminergic neurons by triggering survival pathways in a rat experimental model of Parkinson disease.

Cecropin A is a 37 amino acid chain that functions as an antibacterial and anti-cancer peptide. It is characterized by two alpha helices and has been researched because of the low cytotoxicity produced. Cecropin A produces synergistic effects with some chemotherapeutic agents, enhancing cytotoxic activity.

Cecropin A has been shown to cause bacterial and cancerous cell death by insertion into the cellular membrane due to amphiphilic N-terminal residues. In low lipid to peptide membrane component ratios, cecropin A will form ion channels that will disrupt metabolic gradients and lead to cell death. With high membrane peptide concentrations, cecropin A was observed to aggregate membrane peptides and break the membrane into fragments.

Cecropin B is a 35 amino acid chain that functions as an antibacterial and anti-cancer peptide. It is characterized by two alpha helices and has been researched because of the low cytotoxicity produced. Cecropin B has been shown to produce in vivo cytotoxic effects against stomach carcinomas. It has also been used to synthesize derivatives with activity against other cancer cell lines.

Cecropin B has been shown to cause bacterial and cancerous cell death by insertion into the cellular membrane, which is due to amphiphilic N-terminal residues. In low lipid to peptide membrane component ratios, cecropin B will form ion channels that will disrupt metabolic gradients and lead to cell death. With high membrane peptide concentrations, cecropin B was observed to aggregate membrane peptides and break the membrane into fragments.

Cecropin P1, porcine is a 31 amino acid antibacterial protein that can be isolated from pigs. Cecropin P1 is used as an antibacterial, antifungal and anti-cancer compound. The wide ranging effects of cecropin P1 are properties of its amphipathic N-terminal, lipophilic C-terminal and alpha helical structure. With these structural characteristics, cecropin P1 can bind to the membranes of pathogens and cancerous cells. Cecropin P1 then is inserted into the membrane of the respective cell and disrupts lipid bilayer cohesion, causing rapid membrane degradation and cell lysis.

Cefaclor is a second generation cephalosporin antibiotic isolated from the Acremonium fungus. It targets a wide variety of bacteria including Streptococcus pneumoniae and Haemophilus influenzae and a variety of other gram-negative and gram-positive bacteria. In addition, cefaclor has been useful in studying urinary tract and intra-abdominal infections and the mechanisms of renal transporters hOTA1, hPEPT1, and hPEPT2.

Cefadroxil is a first generation cephalosporin antibiotic with a structure similar to that of cephalexin and cephradine. It targets a wide variety of bacterial species including Staphylococcus and Streptococcus species.

Cefamandole nafate is a second generation cephalosporin antibiotic. It is effective against a variety of gram-negative and gram-positive bacteria. It has been used to study the expression and inhibition of the penicillin binding proteins, especially PBP 2A. Cefamandole nafate is freely soluble in aqueous solution and methanol.

Cefamandole sodium salt is a second generation cephalosporin antibiotic. It is effective against a variety of gram-negative and gram-positive bacteria. It has been used to study the expression and inhibition of the penicillin binding proteins, especially PBP 2A. Cefamandole sodium salt is freely soluble in aqueous solution.

Cefdinir is a third generation cephalosporin antibiotic with resistance to many β-lactamase enzymes. It is effective against gram-positive and gram-negative bacteria. Cefdinir has been used to study infections caused by Staphylococcus aureus and Neisseria gonorrhoeae as well as ftsl gene transfer in H. influenzae. It is an inhibitor of neutrophil myeloperoxidases and exhibits structural similarity to cefixime.

Cefditoren pivoxil is a β-lactam, cephalosporin antibiotic that has shown to be effective against an array of gram positive and negative bacteria. In vitro studies have exhibited cefditoren pixovil to have strong activity towards methicillin and penicillin-susceptible pathogens as well as penicillin-resistant Streptococcus pneumoniae.

Cephalosporins are a type of β-lactam antibiotic consisting of a four-membered β-lactam ring bound to a six-membered dihydrothiazine ring. This two-ring system causes distortion of the β-lactam amide bond, resulting in decreased resonance stabilization and increased reactivity. β-lactams inhibit the formation of peptidoglycan cross-links within bacterial cell walls by targeting penicillin-binding proteins or PBPs. Consequently, the bacterial cell wall becomes weak and cytolysis occurs. Cephalosporin compounds are less susceptible to β-lactamases than the penicillin β-lactam antibiotics.

Antibiotics are often used in clinical in vitro tests known as antimicrobial susceptibility tests or ASTs to determine their efficacy against certain bacterial species. They are tested against gram-negative and gram-positive bacteria using panels, discs, and MIC strips by medical microbiologists. ASTs decrease the risk of using an antibiotic against bacteria exhibiting resistance to it, and the results are used in clinical settings to determine which antibiotic(s) to prescribe for various infections.