Outer membrane porin F (OmpF)

Outer membrane porin F (OmpF) is a major non-specific porin found in the outer membrane of Gram-negative bacteria, most notably Escherichia coli [1]. It functions as a trimeric beta-barrel protein that forms aqueous channels, allowing the passive diffusion of small hydrophilic solutes, such as ions, sugars, and amino acids, into the periplasm [2, 3]. OmpF is clinically significant because it serves as a primary entry route for several classes of antibiotics, including beta-lactams, fluoroquinolones, and tetracyclines [4]. The regulation of OmpF expression is a key factor in bacterial adaptation to environmental stress and antibiotic pressure; for instance, downregulation of OmpF is a common mechanism of high-level antibiotic resistance [5]. Consequently, OmpF is a critical focal point in the study of antimicrobial resistance and the development of next-generation antibiotics designed to optimize membrane penetration [6]. Its structural and functional characteristics are often used as a model for understanding bacterial membrane permeability and the biophysical constraints of drug entry [2, 4].

Other names

Porin OmpFMatrix proteinOuter membrane protein FOmpF porin

Facilitates the passive diffusion of hydrophilic antibiotics across the bacterial outer membrane into the periplasmic space.