Understanding the antimicrobial activity of water soluble γ-cyclodextrin/alamethicin complex

Zhang, Mengke; Wang, Jinpeng; Lyu, Yuan; Fitriyanti, Maya; Hou, Hu; Jin, Zhengyu; Zhu, Xiao; Narsimhan, Ganesan

doi:10.1016/j.colsurfb.2018.08.065

Cited by 14 publications

(7 citation statements)

References 40 publications

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“…In addition, the last 50 ns density profile of total peptides ( Figure 8H, magenta line; Figure 8I, top left) also validates the position of the peptides. Water channel formation has been used as an indicator of pore formation for years [56][57][58][59]. In our MD system, both one-dimensional (1D) density profiles of water and lipid heads ( Figure 8H, blue and black lines) and two-dimensional (2D) density plots ( Figure 8I) clearly show the formation of water channels and membrane deformation.…”

Section: B18 Forms Transmembrane Poresmentioning

confidence: 92%

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Development and Characterization of the Shortest Anti-Adhesion Peptide Analogue of B49Mod1

2020

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Inhibition of cancer cell adhesion is an effective approach to killing adherent cancer cells. B49 and its analog B49Mod1 peptides, derived from the extracellular domain (ECD) of bone marrow stromal antigen 2 (BST-2), display anti-adhesion activity on breast cancer cells. However, the minimal sequence required for this anti-adhesion activity is unknown. Here, we further characterized the anti-adhesion activity of B49Mod1. We show that the anti-adhesion activity of B49Mod1 may require cysteine-linked disulfide bond and that the peptide is susceptible to proteolytic deactivation. Using structure-activity relationship studies, we identified an 18-Mer sequence (B18) as the minimal peptide sequence mediating the anti-adhesion activity of B49Mod1. Atomistic molecular dynamic (MD) simulations reveal that B18 forms a stable complex with the ECD of BST-2 in aqueous solution. MD simulations further reveal that B18 may cause membrane defects that facilitates peptide translocation across the bilayer. Placement of four B18 chains as a transmembrane bundle results in water channel formation, indicating that B18 may impair membrane integrity and form pores. We hereby identify B18 as the minimal peptide sequence required for the anti-adhesion activity of B49Mod1 and provide atomistic insight into the interaction of B18 with BST-2 and the cell membrane.

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Section: B18 Forms Transmembrane Poresmentioning

confidence: 92%

“…Molecular Dynamics (MD) Simulation: The system set up for MD simulations was previously described [59,61,77]. Briefly, the initial structures of two different systems for the MD simulations were constructed using the CHARMM-GUI tool [43,78].…”

Section: Methodsmentioning

confidence: 99%

Development and Characterization of the Shortest Anti-Adhesion Peptide Analogue of B49Mod1

2020

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“…The simulation system setup has been described previously by us [ 11 ] and others [ 17 , 49 , 50 ]. Briefly, for B18L•BST-2 system, two B18L chains were initially placed 5 nm away from the center of BST-2.…”

Section: Methodsmentioning

confidence: 99%

Development of a Cationic Amphiphilic Helical Peptidomimetic (B18L) As A Novel Anti-Cancer Drug Lead

Lyu

Kopcho

Alvarez

et al. 2020

Cancers

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BST-2 is a novel driver of cancer progression whose expression confers oncogenic properties to breast cancer cells. As such, targeting BST-2 in tumors may be an effective therapeutic approach against breast cancer. Here, we sought to develop potent cytotoxic anti-cancer agent using the second-generation BST-2-based anti-adhesion peptide, B18, as backbone. To this end, we designed a series of five B18-derived peptidomimetics. Among these, B18L, a cationic amphiphilic α-helical peptidomimetic, was selected as the drug lead because it displayed superior anti-cancer activity against both drug-resistant and drug-sensitive cancer cells, with minimal toxicity on normal cells. Probing mechanism of action using molecular dynamics simulations, biochemical and membrane biophysics studies, we observed that B18L binds BST-2 and possesses membranolytic characteristics. Furthermore, molecular biology studies show that B18L dysregulates cancer signaling pathways resulting in decreased Src and Erk1/2 phosphorylation, increased expression of pro-apoptotic Bcl2 proteins, caspase 3 cleavage products, as well as processing of the caspase substrate, poly (ADP-ribose) polymerase-1 (PARP-1), to the characteristic apoptotic fragment. These data indicate that through the coordinated regulation of membrane, mitochondrial and signaling events, B18L executes cancer cell death and thus has the potential to be developed into a potent and selective anti-cancer compound.

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“…This invasion method involves several model systems. First is the barrel‐stave model, where peptides having long chains penetrate the bacterial cell membrane forming a pore across the lipid bilayer (Moravej et al, 2018; Sekiya et al, 2018; Zhang et al, 2018). The second one is the toroidal‐pore model, where the peptides are grouped and assembled within the membrane lipids and result in bending from top to bottom, which successively leads to membrane lysis and cell death (Moravej et al, 2018; Xu et al, 2020).…”

Section: Chemistry Of the Antimicrobial Compoundsmentioning

confidence: 99%

Biopolymer‐based antimicrobial coatings for aquatic food products: A review

Chakraborty

Nath

Hoque

et al. 2022

Food Processing Preservation

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Aquatic food products, including fish and crustaceans, are some of the most consumed foods globally and are highly prone to microbial contamination. Such products have been preserved using conventional processing techniques such as freezing, cold storage, modified atmospheric packaging (MAP), and vacuum packaging. However, these techniques have been used since decades and are not cost‐effective. Therefore, alternative sustainable strategies need to be explored. One viable option is the application of biopolymer‐based films and coatings loaded with active antimicrobial agents (peptides and essential oil components) for the preservation of aquatic food products. Nisin is the most widely used peptide for the development of antimicrobial coatings, while eugenol, carvacrol, and cinnamaldehyde are among the most popular essential oil compounds. Findings reveal that both peptides and essential oils, when applied in combination within a coating system, demonstrate robust antimicrobial activity, delayed lipid oxidation, and retain the overall quality of the aquatic food system. Novelty impact statement Antimicrobial‐based coating systems have recently gained worldwide attention due to their ability to delay food contamination and maintain product quality throughout the storage period. This review provides a comprehensive description of peptide and essential oil‐loaded coating systems and their application in the shelf‐life extension of aquatic food products. In addition, the application of nanocomposite systems for the preservation of aquatic foods has been discussed.

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Understanding the antimicrobial activity of water soluble γ-cyclodextrin/alamethicin complex

Cited by 14 publications

References 40 publications

Development and Characterization of the Shortest Anti-Adhesion Peptide Analogue of B49Mod1

Development and Characterization of the Shortest Anti-Adhesion Peptide Analogue of B49Mod1

Development of a Cationic Amphiphilic Helical Peptidomimetic (B18L) As A Novel Anti-Cancer Drug Lead

Biopolymer‐based antimicrobial coatings for aquatic food products: A review

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