Diethylamino hydroxybenzoyl hexyl benzoate (DHHB) is an organic UV filter with high absorption in the UV-A range that minimizes the overexposure of human skin to ultraviolet radiation that may lead to acute and chronic photodamage. In in vitro studies, DHHB was not shown to be mutagenic, clastogenic, or phototoxic. DHHB was approved in Europe in 2005, is also marketed in the U.S., South America, Mexico, Japan and Taiwan, and is used in concentrations up to 10% in sunscreen products, either alone or in combination with other UV absorbers. Only a minor amount of diethylamino hydroxybenzoyl hexyl benzoate will undergo percutaneous absorption and most will remain in the upper layers of the skin. Fluorescence spectroscopy showed that DHHB and avobenzone (another chemical sunscreen ingredient) interact by a static quenching mechanism and DHHB did not affect the avobenzone excited state lifetime.

Florfenicol (Nuflor) is a fluorinated synthetic analog of thiamphenicol. Florfenicol is indicated for the treatment of bovine respiratory disease (BRD) associated with Mannheimia (Pasteurella) haemolytica, Pasteurella multocida, and Haemophilus somnus, for treatment of bovine interdigital phlegmon (foot rot, acute interdigital necrobacillosis, infectious pododermatitis) associated with Fusobacterium necrophorum and Bacteroides melaninogenicus. Florfenicol is a broad-spectrum, primarily bacteriostatic, antibiotic with a range of activity similar to that of chloramphenicol, including many gram-negative and gram-positive organisms; however, florfenicol does not carry the risk of inducing human aplastic anemia that is associated with chloramphenicol. It also has activity against some chloramphenicol resistant strains of bacteria, possibly because it is less affected by the major enzyme produced in plasmid-mediated bacterial resistance against chloramphenicol and thiamphenicol. Although the activity of florfenicol against obligate anaerobes is not addressed in the literature, it is likely to be quite effective. Antibiotic principle of Florfenicol is similar to that of chloramphenicol and Thiamphenicol. Florfenicol inhibits protein synthesis by binding to 70S ribosomal 50S subunits of susceptible bacteria, leading to the inhibition of peptidyl transferase and thereby preventing the transfer of amino acids to extending peptide chains and subsequent protein formation. The bacterial receptor that is the site of action for florfenicol is also considered to be the same as that for chloramphenicol and thiamphenicol. Florfenicol has a fluorine atom instead of the hydroxyl group located at C-3 in the structure of chloramphenicol and thiamphenicol. This prevents the acetylation of bacterial acetyltransferase in this site as to allow florfenicol to be less susceptible to deactivation by bacteria with plasmid-transmissible resistance that involves acetylation of the C-3 hydroxyl group in chloramphenicol and thiamphenicol, and prevents their interaction with bacterial ribosomes.