Human antimicrobial peptides’ antifungal activity against Aspergillus fumigatus

Lupetti, Antonella; Dissel, Jaap T. van; Brouwer, Carlo P.J.M.; Nibbering, Peter H.

doi:10.1007/s10096-008-0553-z

Cited by 51 publications

(27 citation statements)

References 15 publications

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“…The activities of AMPs against lipid-enveloped viruses has been well established, but a full description of their antiviral activities has not been realized [49,50]. Howell et al [51] studied the activities of ceragenins against vaccinia virus.…”

Section: Mechanism Of Actionmentioning

confidence: 99%

“…Antifungal activities of AMPs have been reported, [49,72] and as mimics of AMPs, ceragenins were anticipated to have antifungal activities. Bucki et al [24] determined the antifungal activities of ceragenins CSA-13, CSA-131 and CSA-192 and compared these to those of LL-37, a synthetic, anti-fungal AMP (omiganan) and commonly-used antifungal agents amphotericin B and fluconazole.…”

Section: Anti-fungal Activitymentioning

confidence: 99%

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Ceragenins as Mimics of Endogenous Antimicrobial Peptides

Hashemi¹,

Holden²,

DurnaÅ³

et al. 2017

J Antimicrob Agents

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Ceragenins are small molecule mimics of endogenous antimicrobial peptides (AMPs), and as such display broadspectrum antimicrobial activity. These molecules are derived from a common bile acid and can be prepared at a large scale. Because ceragenins are not peptide based, they are not substrates for proteases. Gram-negative and positive bacteria are susceptible to ceragenins, including drug resistant organisms. Although ceragenins and colistin have common features, ceragenins retain full antibacterial activity against colistin-resistant Gram-negative bacteria. Bactericidal activity of ceragenins involves selective association with bacterial membranes followed by membrane depolarization. Due to this mechanism of action, which provides bactericidal activity against sessile bacteria, ceragenins eradicate established biofilms. Lipid-enveloped viruses (e.g. vaccinia) are deactivated by ceragenins, and topical application of a lead ceragenin decreases transmission of the virus in skin in a murine model. More recently, the activities of ceragenins against fungal pathogens have been reported, with minimum inhibition concentrations comparable to clinically used anti-fungal agents. In addition to antimicrobial activities, ceragenins have been shown to display some of the "secondary" activities attributed to AMPs. In vivo use of ceragenins to eradicate biofilms, prevent infection and accelerate bone growth demonstrate some of the types of applications in which ceragenins may be used to augment or replace activities of endogenous AMPs.

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Section: Mechanism Of Actionmentioning

confidence: 99%

Section: Anti-fungal Activitymentioning

confidence: 99%

Ceragenins as Mimics of Endogenous Antimicrobial Peptides

Hashemi¹,

Holden²,

DurnaÅ³

et al. 2017

J Antimicrob Agents

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“…Despite the high bacterial exposure, infections are rare which suggests highly efficient mechanisms both to protect the host and to maintain a host-microbe balance [1]. Intestine possesses many arms of innate protection from microbial invasion including peristalsis, mucus secretion, low pH, bile salts, digestive enzymes and endogenous antimicrobials [2] including cationic peptides to which acquisition of resistant mutants is less likely to occur [3,4].…”

Section: Introductionmentioning

confidence: 99%

Antimicrobial Activity of Paneth Cells Derived Cryptdin-2 Against Selected Pathogens

Preet¹,

Rishi²

2010

Am. J. Biomed. Sci.

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As cationic antimicrobial peptides are major players of the innate immune response with broad antimicrobial activities, we evaluated the activity of Paneth cells derived cryptdin-2 against selected bacterial pathogens i.e Yersinia enterocolitica, Salmonella typhimurium (Gram negative) and Staphylococcus aureus (Gram positive). Cryptdin(s) preparations were obtained from crypt homogenates as well as from Paneth cells and analyzed using SDS-PAGE. A peptide band corresponding to 3.5 KDa (appx.) was eluted and purity was confirmed using HPLC. It was identified as cryptdin-2 according to its amino acid sequence. The peptide was found to have antimicrobial activity against the selected pathogens as indicated by radial diffusion assay as well as standard colony count technique. However, the activity was found to be the highest for S. aureus. This study thus highlights an important role of cryptdin-2 during host-pathogen interactions and indicates its potential as an inhibitory agent against the enteric infections.

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“…Similarly, two peptide inhibitors of interleukin-10 may be applied to increase anti-hepatitis C virus immune response by restoring the immune stimulatory capabilities of dendritic cells, which have been suppressed by high levels of interleukin-10 [194]. Moreover, candidacidal activities of a synthetic peptide from human lactoferrin fraction 1-11 and 21-31 have been investigated for killing of multidrug-resistant pathogens [195][196][197][198][199]. Present research results, such as phase I safety and tolerability trials of human lactoferrin by AM Pharma [22], indicate that human lactoferrin 1-11 acts by selectively stimulating the innate immune system [200].…”

Section: Commercial Potential Of Milk Derived Proteins and Peptidesmentioning

confidence: 99%