A novel view of lomefloxacin binding to lactoferrin: Spectroscopic approaches

Lactoferrin is an 80 kDa iron-binding glycoprotein found in the saliva, milk, tears, and other exocrine secretions of mammals [1]. It is also released from the specific, secondary granules of neutrophils during inflammatory responses.[2] Lactoferrin exhibits bacteriostatic activity against a wide range of gram-negative and gram-positive bacteria due to its ability to chelate iron, which is essential for microbial growth In addition, lactoferrin exhibits non-iron-dependent antibacterial, antifungal, antiviral, antitumor, anti-inflammatory, and immune regulatory activities [3,4]. It constitutes an important component of the innate immune system and may represent a novel therapeutic with broad spectrum potential. Lomefloxacin is a fluoroquinolone antibiotic that kills certain bacteria or stops their growth. It treats respiratory and urinary tract infection, or prevents infection during surgery on urinary tract. Lomefloxacin is taken orally, usually daily for 10-14 days. The pharmacokinetic properties of this drug include good oral absorption and long half-life [5]. Inthis paper the binding reaction of lomefloxacin to human lactoferrin has been investigated by multi spectroscopic study (UV spectra, Fluorescence spectra and Circular dichroism spectroscopy).