Development of anti-bacterial surfaces using a hydrophobin chimeric protein

Sorrentino, Ilaria; Gargano, Marika; Ricciardelli, Annarita; Parrilli, Ermenegilda; Buonocore, Carmine; Pascale, Donatella de; Giardina, Paola; Piscitelli, Alessandra

doi:10.1016/j.ijbiomac.2020.07.301

Cited by 13 publications

(8 citation statements)

References 41 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Peptide immobilization techniques provide a means to overcome some of the challenges associated with LL-37, including cytotoxicity and low stability in physiological environments [131][132][133][134]. Immobilization may increase the ability of LL-37 to inhibit the colonization and biofilm formation of bacteria [131,132,134], and thus immobilization techniques are utilized in wound environments [131] and medical devices [132].…”

Section: Immobilization Techniques and Ll-37 Delivery Systemsmentioning

confidence: 99%

The Potential of Human Peptide LL-37 as an Antimicrobial and Anti-Biofilm Agent

2021

View full text Add to dashboard Cite

The rise in antimicrobial resistant bacteria threatens the current methods utilized to treat bacterial infections. The development of novel therapeutic agents is crucial in avoiding a post-antibiotic era and the associated deaths from antibiotic resistant pathogens. The human antimicrobial peptide LL-37 has been considered as a potential alternative to conventional antibiotics as it displays broad spectrum antibacterial and anti-biofilm activities as well as immunomodulatory functions. While LL-37 has shown promising results, it has yet to receive regulatory approval as a peptide antibiotic. Despite the strong antimicrobial properties, LL-37 has several limitations including high cost, lower activity in physiological environments, susceptibility to proteolytic degradation, and high toxicity to human cells. This review will discuss the challenges associated with making LL-37 into a viable antibiotic treatment option, with a focus on antimicrobial resistance and cross-resistance as well as adaptive responses to sub-inhibitory concentrations of the peptide. The possible methods to overcome these challenges, including immobilization techniques, LL-37 delivery systems, the development of LL-37 derivatives, and synergistic combinations will also be considered. Herein, we describe how combination therapy and structural modifications to the sequence, helicity, hydrophobicity, charge, and configuration of LL-37 could optimize the antimicrobial and anti-biofilm activities of LL-37 for future clinical use.

show abstract

Section: Immobilization Techniques and Ll-37 Delivery Systemsmentioning

confidence: 99%

The Potential of Human Peptide LL-37 as an Antimicrobial and Anti-Biofilm Agent

2021

View full text Add to dashboard Cite

show abstract

“…They discourage accumulation and adsorption onto the surface, therefore effectively inhibiting bacterial adhesion and thus biofilm formation onto the hyphae, spores, or other biofilm surfaces [Wick et al, 2007;Artini et al, 2017]. In fact, new developments in antibacterial surfaces with application in, for example, medical devices, include the use of recombinant hydrophobins to prevent biofilm attachment [Wang et al, 2017;Berger and Sallada, 2019;Devine et al, 2019;Sorrentino et al, 2020].…”

Section: Hydrophobic Surface Formationmentioning

confidence: 99%

Amyloid Proteins in Plant-Associated Microbial Communities

et al. 2021

View full text Add to dashboard Cite

Amyloids have proven to be a widespread phenomenon rather than an exception. Many proteins presenting the hallmarks of this characteristic beta sheet-rich folding have been described to date. Particularly common are functional amyloids that play an important role in the promotion of survival and pathogenicity in prokaryotes. Here, we describe important developments in amyloid protein research that relate to microbe-microbe and microbe-host interactions in the plant microbiome. Starting with biofilms, which are a broad strategy for bacterial persistence that is extremely important for plant colonization. Microbes rely on amyloid-based mechanisms to adhere and create a protective coating that shelters them from external stresses and promotes cooperation. Another strategy generally carried out by amyloids is the formation of hydrophobic surface layers. Known as hydrophobins, these proteins coat the aerial hyphae and spores of plant pathogenic fungi, as well as certain bacterial biofilms. They contribute to plant virulence through promoting dissemination and infectivity. Furthermore, antimicrobial activity is an interesting outcome of the amyloid structure that has potential application in medicine and agriculture. There are many known antimicrobial amyloids released by animals and plants; however, those produced by bacteria or fungi remain still largely unknown. Finally, we discuss amyloid proteins with a more indirect mode of action in their host interactions. These include virulence-promoting harpins, signaling transduction that functions through amyloid templating, and root nodule bacteria proteins that promote plant-microbe symbiosis. In summary, amyloids are an interesting paradigm for their many functional mechanisms linked to bacterial survival in plant-associated microbial communities.

show abstract

“…Nevertheless, very few options are available for the treatment of urinary biofilm-associated infections. For example, modified catheters and implants based on hydrogel, Poly (Tetralfouroethalene) (PTFE) coatings, Polyzwitterions coatings, and Poly (Ethylene Glycol) (PEG) coatings could be useful for the prevention of fouling [2,40], while a number of electrophysical and electrochemical approaches targeting already-formed biofilms have recently been proposed [41].…”

Section: Introductionmentioning

confidence: 99%

Improving the Efficacy of Antimicrobials against Biofilm-Embedded Bacteria Using Bovine Hyaluronidase Azoximer (Longidaza®)

et al. 2021

View full text Add to dashboard Cite

While in a biofilm, bacteria are extremely resistant to both antimicrobials and the immune system, leading to the development of chronic infection. Here, we show that bovine hyaluronidase fused with a copolymer of 1,4-ethylenepiperazine N-oxide and (N-carboxymethyl) -1,4-ethylenepiperazinium bromide (Longidaza®) destroys both mono- and dual-species biofilms formed by various bacteria. After 4 h of treatment with 750 units of the enzyme, the residual biofilms of Staphylococcus aureus, Enterococcus faecalis, Escherichia coli, Pseudomonas aeruginosa and Klebsiella pneumoniae preserved about 50–70% of their initial mass. Biomasses of dual-species biofilms formed by S. aureus and the four latter species were reduced 1.5-fold after 24 h treatment, while the significant destruction of S. aureus–P. aeruginosa and S. aureus–K. pneumoniae was also observed after 4 h of treatment with Longidaza®. Furthermore, when applied in combination, Longidaza® increased the efficacy of various antimicrobials against biofilm-embedded bacteria, although with various increase-factor values depending on both the bacterial species and antimicrobials chosen. Taken together, our data indicate that Longidaza® destroys the biofilm structure, facilitating the penetration of antimicrobials through the biofilm, and in this way improving their efficacy, lowering the required dose and thus also potentially reducing the associated side effects.

show abstract

Development of anti-bacterial surfaces using a hydrophobin chimeric protein

Cited by 13 publications

References 41 publications

The Potential of Human Peptide LL-37 as an Antimicrobial and Anti-Biofilm Agent

The Potential of Human Peptide LL-37 as an Antimicrobial and Anti-Biofilm Agent

Amyloid Proteins in Plant-Associated Microbial Communities

Improving the Efficacy of Antimicrobials against Biofilm-Embedded Bacteria Using Bovine Hyaluronidase Azoximer (Longidaza®)

Contact Info

Product

Resources

About