2021
DOI: 10.1038/s41429-021-00406-5
|View full text |Cite
|
Sign up to set email alerts
|

In vitro and in vivo antibacterial properties of peptide AMC-109 impregnated wound dressings and gels

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

0
11
0

Year Published

2022
2022
2024
2024

Publication Types

Select...
8
1

Relationship

3
6

Authors

Journals

citations
Cited by 14 publications
(12 citation statements)
references
References 53 publications
0
11
0
Order By: Relevance
“…This because the amino acid sequence variation, the tether chemistry, and the tether attachment point on the AMP are known to strongly influence the activity of the grafted AMPs. ,, The minimalistic approach is suitable considering the scope of the study; it should however be emphasized that the design may not be optimal for other applications. As basis for the coating, we chose to use AMC-109 (also known as LTX-109), which is a synthetic tripeptide AMP that has proven efficient against common bacterial and fungal pathogens. Its primary structure corresponds to R–W–R, giving the peptide a net charge of +3. The central tryptophan is modified with three bulky tert -butyl groups, and the C-terminal is capped with an ethylphenyl group, which enhances the overall hydrophobicity of the peptide and protects it against enzymatic digestion , (Figure a).…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…This because the amino acid sequence variation, the tether chemistry, and the tether attachment point on the AMP are known to strongly influence the activity of the grafted AMPs. ,, The minimalistic approach is suitable considering the scope of the study; it should however be emphasized that the design may not be optimal for other applications. As basis for the coating, we chose to use AMC-109 (also known as LTX-109), which is a synthetic tripeptide AMP that has proven efficient against common bacterial and fungal pathogens. Its primary structure corresponds to R–W–R, giving the peptide a net charge of +3. The central tryptophan is modified with three bulky tert -butyl groups, and the C-terminal is capped with an ethylphenyl group, which enhances the overall hydrophobicity of the peptide and protects it against enzymatic digestion , (Figure a).…”
Section: Resultsmentioning
confidence: 99%
“…Most studied AMPs have a natural origin as being part of the innate defense of different prokaryotic or eukaryotic species. , The use of natural AMPs for antibacterial products has however been marginally successful; their length and the dependence on native sequence for their function makes them sensitive to environmental settings and to enzymatic digestion, prone to cause off-target cytotoxicity and lead to high production cost . Through studies of the structure–activity relationship for natural AMPs, novel peptides that are smaller, cheaper, and more stable have been designed. The smallest pharmacophore was found to have only three residues and has proven to be a good candidate for usage in AMP-based therapies and products against common bacterial and fungal pathogens. …”
Section: Introductionmentioning
confidence: 99%
“…109 In another work, AMP AMC-109 impregnated cotton wound dressings displayed a seven-log reduction of S. aureus and MRSA compared to commercial drugs (Altargo and Fucidin cream) in an in vivo wound model. 205 This journal © The Royal Society of Chemistry 2022…”
Section: Amp-based Npsmentioning
confidence: 99%
“…In a study of a novel synthetic cationic peptide, AMC-19, effective antimicrobial results were reported in a MRSA-induced wound infection [ 71 ]. Results also showed high stability of AMC-19 with a 7-fold reduced bacterial load in 3 days, demonstrating its potential against MRSA via topical administration [ 72 ]. Because of their low activity, nonspecific cytotoxicity and susceptibility to proteolysis, ongoing studies aim to further develop a second generation of AMPs.…”
Section: Reviewmentioning
confidence: 99%