scholarly journals Architectural Effects of Star-Shaped “Structurally Nanoengineered Antimicrobial Peptide Polymers” (SNAPPs) on Their Biological Activity

2018 ◽  
Vol 7 (21) ◽  
pp. 1800627 ◽  
Author(s):  
Steven J. Shirbin ◽  
Ignacio Insua ◽  
James A. Holden ◽  
Jason C. Lenzo ◽  
Eric C. Reynolds ◽  
...  
Keyword(s):  
Biological Activity ◽  
Antimicrobial Peptide ◽  
Peptide Polymers ◽  
Architectural Effects

scholarly journals Structurally nanoengineered antimicrobial peptide polymers: design, synthesis and biomedical applications

2021 ◽  
Vol 37 (8) ◽  
Author(s):  
Ronisha Ramamurthy ◽  
Chetan H. Mehta ◽  
Usha Y. Nayak
Keyword(s):  
Health Care ◽  
Antimicrobial Peptide ◽  
Biomedical Applications ◽  
Multidrug Resistant ◽  
Chronic Infections ◽  
Synthesis Mechanism ◽  
Design Synthesis ◽  
Global Health Care ◽  
Conventional Antibiotics ◽  
Peptide Polymers

Abstract Antimicrobial resistance not only increases the contagiousness of infectious diseases but also a threat for the future as it is one of the health care concern around the globe. Conventional antibiotics are unsuccessful in combating chronic infections caused by multidrug-resistant (MDR) bacteria, therefore it is important to design and develop novel strategies to tackle this problems. Among various novel strategies, Structurally Nanoengineered Antimicrobial Peptide Polymers (SNAPPs) have been introduced in recent years to overcome this global health care issue and they are found to be more efficient in their performance. Many facile methods are adapted to synthesize complex SNAPPs with required dimensions and unique functionalities. Their unique characteristics and remarkable properties have been exploited for their immense applications in various fields including biomedicine, targeting therapies, gene delivery, bioimaging, and many more. This review article deals with its background, design, synthesis, mechanism of action, and wider applications in various fields of SNAPPs. Graphic abstract

Immobilization and Intracellular Delivery of Structurally Nanoengineered Antimicrobial Peptide Polymers Using Polyphenol‐Based Capsules

2021 ◽  
pp. 2107341
Author(s):  
Jiaying Song ◽  
Christina Cortez‐Jugo ◽  
Steven J. Shirbin ◽  
Zhixing Lin ◽  
Shuaijun Pan ◽  
...  
Keyword(s):  
Antimicrobial Peptide ◽  
Intracellular Delivery ◽  
Peptide Polymers

scholarly journals Effects of Dimerization on the Structure and Biological Activity of Antimicrobial Peptide Ctx-Ha

2012 ◽  
Vol 56 (6) ◽  
pp. 3004-3010 ◽  
Author(s):  
E. N. Lorenzón ◽  
G. F. Cespedes ◽  
E. F. Vicente ◽  
L. G. Nogueira ◽  
T. M. Bauab ◽  
...  
Keyword(s):  
Antimicrobial Activity ◽  
Biological Activity ◽  
Antimicrobial Peptide ◽  
Hemolytic Activity ◽  
Pore Diameter ◽  
Solid Phase ◽  
Biological Activities ◽  
Solid Phase Peptide Synthesis ◽  
Activity Assay ◽  
Growth Of Bacteria

ABSTRACTIt is well known that cationic antimicrobial peptides (cAMPs) are potential microbicidal agents for the increasing problem of antimicrobial resistance. However, the physicochemical properties of each peptide need to be optimized for clinical use. To evaluate the effects of dimerization on the structure and biological activity of the antimicrobial peptide Ctx-Ha, we have synthesized the monomeric and three dimeric (Lys-branched) forms of the Ctx-Ha peptide by solid-phase peptide synthesis using a combination of 9-fluorenylmethyloxycarbonyl (Fmoc) andt-butoxycarbonyl (Boc) chemical approaches. The antimicrobial activity assay showed that dimerization decreases the ability of the peptide to inhibit growth of bacteria or fungi; however, the dimeric analogs displayed a higher level of bactericidal activity. In addition, a dramatic increase (50 times) in hemolytic activity was achieved with these analogs. Permeabilization studies showed that the rate of carboxyfluorescein release was higher for the dimeric peptides than for the monomeric peptide, especially in vesicles that contained sphingomyelin. Despite different biological activities, the secondary structure and pore diameter were not significantly altered by dimerization. In contrast to the case for other dimeric cAMPs, we have shown that dimerization selectively decreases the antimicrobial activity of this peptide and increases the hemolytic activity. The results also show that the interaction between dimeric peptides and the cell wall could be responsible for the decrease of the antimicrobial activity of these peptides.

scholarly journals Antimicrobial peptide polymers: no escape to ESKAPE pathogens—a review

2020 ◽  
Vol 36 (9) ◽  
Author(s):  
Songhita Mukhopadhyay ◽  
A. S. Bharath Prasad ◽  
Chetan H. Mehta ◽  
Usha Y. Nayak
Keyword(s):  
Antimicrobial Peptide ◽  
Peptide Polymers ◽  
Eskape Pathogens

NOVEL FAMILY OF PROLINE-RICH ANTIMICROBIAL PEPTIDES INHIBITING BACTERIAL TRANSLATION

2021 ◽  
Vol 1 (19) ◽  
pp. 173-174
Author(s):  
R.N. Kruglikov ◽  
T.V. Ovchinnikova ◽  
P.V. Panteleev
Keyword(s):  
Biological Activity ◽  
Antimicrobial Peptides ◽  
Antimicrobial Peptide ◽  
Bacterial Cells ◽  
Bacterial Translation

A new proline-rich antimicrobial peptide from alpaca (Vicugnia pacos) was obtained, as well as its modified analogs. The biological activity of the peptides was studied, and also the role of the N- and C-terminal fragments, when acting on bacterial cells, was analyzed.

scholarly journals Structure-Activity Relationship of Synthetic Variants of the Milk-Derived Antimicrobial Peptide αs2-Casein f(183–207)

2013 ◽  
Vol 79 (17) ◽  
pp. 5179-5185 ◽  
Author(s):  
Avelino Alvarez-Ordóñez ◽  
Máire Begley ◽  
Tanya Clifford ◽  
Thérèse Deasy ◽  
Kiera Considine ◽  
...  
Keyword(s):  
Amino Acids ◽  
Biological Activity ◽  
Amino Acid ◽  
Antimicrobial Peptide ◽  
Peptide Sequence ◽  
Content Type ◽  
Charged Amino Acids ◽  
Food Borne ◽  
Relationship Of ◽  
Positively Charged

ABSTRACTTemplate-based studies on antimicrobial peptide (AMP) derivatives obtained through manipulation of the amino acid sequence are helpful to identify properties or residues that are important for biological activity. The present study sheds light on the importance of specific amino acids of the milk-derived αs2-casein f(183–207) peptide to its antibacterial activity against the food-borne pathogensListeria monocytogenesandCronobacter sakazakii. Trimming of the peptide revealed that residues at the C-terminal end of the peptide are important for activity. Removal of the last 5 amino acids at the C-terminal end and replacement of the Arg at position 23 of the peptide sequence by an Ala residue significantly decreased activity. These findings suggest that Arg23 is very important for optimal activity of the peptide. Substitution of the also positively charged Lys residues at positions 15 and 17 of the αs2-casein f(183–207) peptide also caused a significant reduction of the effectiveness againstC. sakazakii, which points toward the importance of the positive charge of the peptide for its biological activity. Indeed, simultaneous replacement of various positively charged amino acids was linked to a loss of bactericidal activity. On the other hand, replacement of Pro residues at positions 14 and 20 resulted in a significantly increased antibacterial potency, and hydrophobic end tagging of αs2-casein f(193–203) and αs2-casein f(197–207) peptides with multiple Trp or Phe residues significantly increased their potency againstL. monocytogenes. Finally, the effect of pH (4.5 to 7.4), temperature (4°C to 37°C), and addition of sodium and calcium salts (1% to 3%) on the activity of the 15-amino-acid αs2-casein f(193–207) peptide was also determined, and its biological activity was shown to be completely abolished in high-saline environments.

scholarly journals Shortened derivatives from native antimicrobial peptide LyeTx I: In vitro and in vivo biological activity assessment

2020 ◽  
pp. 153537022096696
Author(s):  
Leonardo Lima Fuscaldi ◽  
Joaquim Teixeira de Avelar Júnior ◽  
Daniel Moreira dos Santos ◽  
Daiane Boff ◽  
Vívian Louise Soares de Oliveira ◽  
...  
Keyword(s):  
Biological Activity ◽  
Antimicrobial Peptide ◽  
Mammalian Cells ◽  
Antimicrobial Agents ◽  
Sodium Dodecyl ◽  
Alpha Helix ◽  
In Vitro Assays ◽  
Control Group

In the continuing search for novel antibiotics, antimicrobial peptides are promising molecules, due to different mechanisms of action compared to classic antibiotics and to their selectivity for interaction with microorganism cells rather than with mammalian cells. Previously, our research group has isolated the antimicrobial peptide LyeTx I from the venom of the spider Lycosa erythrognatha. Here, we proposed to synthesize three novel shortened derivatives from LyeTx I (LyeTx I mn; LyeTx I mnΔK; LyeTx I mnΔKAc) and to evaluate their toxicity and biological activity as potential antimicrobial agents. Peptides were synthetized by Fmoc strategy and circular dichroism analysis was performed, showing that the three novel shortened derivatives may present membranolytic activity, like the original LyeTx I, once they folded as an alpha helix in 2.2.2-trifluorethanol and sodium dodecyl sulfate. In vitro assays revealed that the shortened derivative LyeTx I mnΔK presents the best score between antimicrobial (↓ MIC) and hemolytic (↑ EC50) activities among the synthetized shortened derivatives, and LUHMES cell-based NeuriTox test showed that it is less neurotoxic than the original LyeTx I (EC50 [LyeTx I mnΔK] ⋙ EC50 [LyeTx I]). In vivo data, obtained in a mouse model of septic arthritis induced by Staphylococcus aureus, showed that LyeTx I mnΔK is able to reduce infection, as demonstrated by bacterial recovery assay (∼10-fold reduction) and scintigraphic imaging (less technetium-99m labeled-Ceftizoxime uptake by infectious site). Infection reduction led to inflammatory process and pain decreases, as shown by immune cells recruitment reduction and threshold nociception increment, when compared to positive control group. Therefore, among the three shortened peptide derivatives, LyeTx I mnΔK is the best candidate as antimicrobial agent, due to its smaller amino acid sequence and toxicity, and its greater biological activity.

Combating multidrug-resistant Gram-negative bacteria with structurally nanoengineered antimicrobial peptide polymers

2016 ◽  
Vol 1 (11) ◽  
Author(s):  
Shu J. Lam ◽  
Neil M. O'Brien-Simpson ◽  
Namfon Pantarat ◽  
Adrian Sulistio ◽  
Edgar H. H. Wong ◽  
...  
Keyword(s):  
Antimicrobial Peptide ◽  
Multidrug Resistant ◽  
Gram Negative Bacteria ◽  
Gram Negative ◽  
Peptide Polymers

Improving the biological activity of the antimicrobial peptide anoplin by membrane anchoring through a lipophilic amino acid derivative

2013 ◽  
Vol 23 (13) ◽  
pp. 3749-3752 ◽  
Author(s):  
Jack C. Slootweg ◽  
Timo B. van Schaik ◽  
H. (Linda) C. Quarles van Ufford ◽  
Eefjan Breukink ◽  
Rob M.J. Liskamp ◽  
...  
Keyword(s):  
Biological Activity ◽  
Amino Acid ◽  
Antimicrobial Peptide ◽  
Acid Derivative ◽  
Amino Acid Derivative ◽  
Membrane Anchoring

Plasma Corona Protects Human Immune Cells from Structurally Nanoengineered Antimicrobial Peptide Polymers

2021 ◽  
Author(s):  
Alessia C. G. Weiss ◽  
Steven J. Shirbin ◽  
Hannah G. Kelly ◽  
Quinn A. Besford ◽  
Stephen J. Kent ◽  
...  
Keyword(s):  
Antimicrobial Peptide ◽  
Immune Cells ◽  
Plasma Corona ◽  
Human Immune ◽  
Peptide Polymers
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