## 2 Discussion
The porins that have been shown to play a direct role or have shown interaction with antibiotics are HMP-PA [46],Omp-PD [46], Omp-SL [46], HMP-AB [46],/CarO isoforms [155; 156; 157], rOprD homologue [158], OccAB1-OccAB4 [159], DcaP [22], Omp-ECB [46], OmpF and OmpC [22; 24; 26; 38; 39; 44; 48; 51; 53; 55; 61; 67; 72; 74; 79; 81; 82; 83; 84; 87; 89; 90; 91; 92; 93; 94; 95; 96; 97; 98; 99; 98; 99; 99; 99; 99; 99; 99; 100; 10; 101; 102; 103; 104; 105; 106; 107; 108; 109; 111; 112; 113; 114; 115; 116; 117; 118; 119; 120; 121; 122; 123; 124; 124; 125; 126; 127; 128; 129; 130; 131; 132; 133; 134; 135; 136; 137; 138; 139; 140; 141; 142; 143; 144; 145; 146; 147; 148; 149; 150; 151; 152; 153; 154; 155; 15694-96,99-102,104-107,109,112,177] Omp35, Omp36 [113-118,177], OmpE36 and OmpE35 [23], OmpK36, OmpK35 [112,113,122], OmpPst1/OmpPst2 [119,121]/OprO, Oprp [123,165], OprD [140-144], OccD3 [42], OccK1, OccK2 [135], Occk8(OprE) [164]. From the studies it has been shown that the transport of Fosfomycin occurs through OmpF porins [76], while the transport of Cephalosporin occurs through OmpF and OmpC porins [23]. Fosfomycin, and Fosmidomycin transport through OprO/OprP [123,165] porins, and the dynamics of loop L3 from OmpF have been demonstrated to influence antibiotic translocation [48,101]. Additionally, ampicillin permeation has been demonstrated to occur through the major outer-membrane channel OmpF [26,54,181], and the fluoro-quinolones interaction in conjunction with magnesium ions thru OmpF, OmpC, Omp36, and Omp35 porins [177]. Furthermore, Kanamycin and other aminoglycos (see also Table 3) transport/uptake into the bacterium peremptorily facilitated by OmpF/OmpC channels [39], and the transport of small beta-lactamase inhibitors through OmpF/OmpC [26,37] (see Table 3) for other molecule/omps flux rates). As it is challenging to measure the flux of these tiny molecules, reported turnover rates molecules/second (Table 3) at a given concentration gradient for different outer membrane proteins (Omps) with different substrates have been given [26,27,39,54,153]. In general, these studies have provided insights into the explicit role of outer membrane proteins/porins/channels/transporters in the haulage of antibiotics and have highlighted the importance of these proteins in the efficacy of antibiotic therapy. Targeting these porins may provide a promising strategy for advancing and improving novel current antimicrobial/antibiotic agents and therapy. However, further extensive research and data sets are needed to comprehend the mechanisms and systems involved in antibiotic transport through porins. Further to fully identify new targets for the progress of novel antimicrobial strategies. Electrophysiology techniques, such as planar lipid bilayer, have provided valuable insights into Membrane channels' structural and functional properties [7,24,29,49]. These techniques have also been used to examine the interface of antibiotics with the pore-forming complex, providing a molecular-level understanding of the transport mechanisms [7,24,29,37,42,49]. Despite these advances, a significant amount of information has been gathered toward understanding the correlation between pore geometry and antibiotic transport using electro-physiology alone [24,37,42,47,48,51,54,55,75,76,78,79,83,87,96,98,124,134,153,177]. Furthermore, the molecular transport mechanism through membrane channels is essential in developing targeted therapies against antimicrobial resistance [15,24]. Understanding how antibiotics interact with the bacteria at a molecular level makes it possible to design strategies that increase permeation and avoid resistance mechanisms based on decreased permeability. This can further take the lead toward the development of more efficient antibiotic therapeutics and systems to combat bacterial resistance [7,15,24,29,49]. It is also vital to note that the study of membrane channels is not constrained to their role in antimicrobial resistance.