scholarly journals Cell Surface Binding and Lipid Interactions behind Chemotherapy-Drug-Induced Ion Pore Formation in Membranes

Membranes ◽  
2021 ◽  
Vol 11 (7) ◽  
pp. 501
Author(s):  
Md. Ashrafuzzaman ◽  
Zahid Khan ◽  
Ashwaq Alqarni ◽  
Mohammad Alanazi ◽  
Mohammad Shahabul Alam

Chemotherapy drugs (CDs) disrupt the lipid membrane’s insulation properties by inducing stable ion pores across bilayer membranes. The underlying molecular mechanisms behind pore formation have been revealed in this study using several methods that confirm molecular interactions and detect associated energetics of drugs on the cell surface in general and in lipid bilayers in particular. Liposome adsorption and cell surface binding of CD colchicine has been demonstrated experimentally. Buffer dissolved CDs were considerably adsorbed in the incubated phospholipid liposomes, measured using the patented ‘direct detection method’. The drug adsorption process is regulated by the membrane environment, demonstrated in cholesterol-containing liposomes. We then detailed the phenomenology and energetics of the low nanoscale dimension cell surface (membrane) drug distribution, using atomic force microscopy (AFM) imaging what addresses the surface morphology and measures adhesion force (reducible to adhesive energy). Liposome adsorption and cell surface binding data helped model the cell surface drug distribution. The underlying molecular interactions behind surface binding energetics of drugs have been addressed in silico numerical computations (NCs) utilizing the screened Coulomb interactions among charges in a drug–drug/lipid cluster. Molecular dynamics (MD) simulations of the CD-lipid complexes detected primarily important CD-lipid electrostatic and van der Waals (vdW) interaction energies. From the energetics point of view, both liposome and cell surface membrane adsorption of drugs are therefore obvious findings. Colchicine treated cell surface AFM images provide a few important phenomenological conclusions, such as drugs bind generally with the cell surface, bind independently as well as in clusters of various sizes in random cell surface locations. The related adhesion energy decreases with increasing drug cluster size before saturating for larger clusters. MD simulation detected electrostatic and vdW and NC-derived charge-based interactions explain molecularly of the cause of cell surface binding of drugs. The membrane binding/association of drugs may help create drug–lipid complexes with specific energetics and statistically lead to the creation of ion channels. We reveal here crucial molecular understanding and features of the pore formation inside lipid membranes that may be applied universally for most of the pore-forming existing agents and novel candidate drugs.

Biomolecules ◽  
2020 ◽  
Vol 10 (8) ◽  
pp. 1144
Author(s):  
Makoto Ono ◽  
Don E. Burgess ◽  
Elizabeth A. Schroder ◽  
Claude S. Elayi ◽  
Corey L. Anderson ◽  
...  

Significant advances in our understanding of the molecular mechanisms that cause congenital long QT syndrome (LQTS) have been made. A wide variety of experimental approaches, including heterologous expression of mutant ion channel proteins and the use of inducible pluripotent stem cell-derived cardiomyocytes (iPSC-CMs) from LQTS patients offer insights into etiology and new therapeutic strategies. This review briefly discusses the major molecular mechanisms underlying LQTS type 2 (LQT2), which is caused by loss-of-function (LOF) mutations in the KCNH2 gene (also known as the human ether-à-go-go-related gene or hERG). Almost half of suspected LQT2-causing mutations are missense mutations, and functional studies suggest that about 90% of these mutations disrupt the intracellular transport, or trafficking, of the KCNH2-encoded Kv11.1 channel protein to the cell surface membrane. In this review, we discuss emerging strategies that improve the trafficking and functional expression of trafficking-deficient LQT2 Kv11.1 channel proteins to the cell surface membrane and how new insights into the structure of the Kv11.1 channel protein will lead to computational approaches that identify which KCNH2 missense variants confer a high-risk for LQT2.


2020 ◽  
Author(s):  
Vikas D. Trivedi ◽  
Nikhil U. Nair

AbstractAntimicrobial peptides (AMPs) have gained attention recently due to increasing antibiotic resistance amongst pathogens. Most AMPs are cationic in nature and their preliminary interactions with the negatively charged cell surface is mediated by electrostatic attraction. This is followed by pore formation, which is either receptor-dependent or -independent and leads to cell death. Typically, AMPs are characterized by their killing activity using bioactivity assays to determine host range and degree of killing. However, cell surface binding is independent from killing. Most of the studies performed to-date have attempted to quantify the peptide binding using artificial membranes. Here, we use the narrow-spectrum class IIa bacteriocin AMP pediocin PA-1 conjugated to a fluorescent dye as a probe to monitor cell surface binding. We developed a flow cytometry-based assay to quantify the strength of binding in target and non-target species. Through our binding assays, we found a strong positive correlation between cell surface charge and pediocin PA-1 binding. Interestingly, we also found inverse correlation between zeta potential and pediocin PA-1 binding, the correlation coefficient for which improved when only Gram-positives were considered. We also show the effect of the presence of protein, salt, polycationic species, and other non-target species on the binding of pediocin PA-1 to the target organism. We conclude that the of presence of highly charged non-target species, as well as solutes, can decrease the binding, and the apparent potency, of pediocin PA-1. Thus, these outcomes are highly significant to the use of pediocin PA-1 and related AMPs in mixed microbial settings such as those found in the gut microbiota.


1993 ◽  
Vol 268 (7) ◽  
pp. 5279-5284
Author(s):  
B.S. Weeks ◽  
K. Desai ◽  
P.M. Loewenstein ◽  
M.E. Klotman ◽  
P.E. Klotman ◽  
...  

1991 ◽  
Vol 266 (28) ◽  
pp. 18655-18659 ◽  
Author(s):  
P.F. Blackmore ◽  
J. Neulen ◽  
F. Lattanzio ◽  
S.J. Beebe

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