scholarly journals Self-assembly dynamics and antimicrobial activity of all l- and d-amino acid enantiomers of a designer peptide

Nanoscale ◽  
2019 ◽  
Vol 11 (1) ◽  
pp. 266-275 ◽  
Author(s):  
Zhou Ye ◽  
Xiao Zhu ◽  
Sergio Acosta ◽  
Dhiraj Kumar ◽  
Ting Sang ◽  
...  
Keyword(s):  
Antimicrobial Activity ◽  
Amino Acid ◽  
Antimicrobial Peptides ◽  
Self Assembly ◽  
Amino Acid Enantiomers

All l- and d-antimicrobial peptides had different self-assembly dynamics with implication in their antimicrobial activity.

scholarly journals Primary Structure Analysis of Antifungal Peptides from Cultivated and Wild Cereals

Plants ◽  
2018 ◽  
Vol 7 (3) ◽  
pp. 74 ◽  
Author(s):  
Eugene Rogozhin ◽  
Dmitry Ryazantsev ◽  
Alexey Smirnov ◽  
Sergey Zavriev
Keyword(s):  
Antimicrobial Activity ◽  
Amino Acid ◽  
Antifungal Activity ◽  
Antimicrobial Peptides ◽  
Structure Analysis ◽  
Primary Structure ◽  
Biologically Active ◽  
Amino Acid Residues ◽  
Wild Cereals ◽  
Determining Factor

Cereal-derived bioactive peptides with antimicrobial activity have been poorly explored compared to those from dicotyledonous plants. Furthermore, there are a few reports addressing the structural differences between antimicrobial peptides (AMPs) from cultivated and wild cereals, which may shed light on significant varieties in the range and level of their antimicrobial activity. We performed a primary structure analysis of some antimicrobial peptides from wild and cultivated cereals to find out the features that are associated with the much higher antimicrobial resistance characteristic of wild plants. In this review, we identified and analyzed the main parameters determining significant antifungal activity. They relate to a high variability level in the sequences of C-terminal fragments and a high content of hydrophobic amino acid residues in the biologically active defensins in wild cereals, in contrast to AMPs from cultivated forms that usually exhibit weak, if any, activity. We analyzed the similarity of various physicochemical parameters between thionins and defensins. The presence of a high divergence on a fixed part of any polypeptide that is close to defensins could be a determining factor. For all of the currently known hevein-like peptides of cereals, we can say that the determining factor in this regard is the structure of the chitin-binding domain, and in particular, amino acid residues that are not directly involved in intermolecular interaction with chitin. The analysis of amino acid sequences of alpha-hairpinins (hairpin-like peptides) demonstrated much higher antifungal activity and more specificity of the peptides from wild cereals compared with those from wheat and corn, which may be associated with the presence of a mini cluster of positively charged amino acid residues. In addition, at least one hydrophobic residue may be responsible for binding to the components of fungal cell membranes.

scholarly journals Metal self-assembly mimosine peptides with enhanced antimicrobial activity: towards a new generation of multitasking chelating agents

2020 ◽  
Vol 49 (9) ◽  
pp. 2862-2879 ◽  
Author(s):  
Joanna Izabela Lachowicz ◽  
Gabriele Dalla Torre ◽  
Rosita Cappai ◽  
Enrico Randaccio ◽  
Valeria M. Nurchi ◽  
...  
Keyword(s):  
Antimicrobial Activity ◽  
Amino Acid ◽  
Self Assembly ◽  
Building Block ◽  
Chelating Agents ◽  
Metal Coordination ◽  
Protein Amino Acid ◽  
Coordination Ability ◽  
New Generation

Mimosine is a non-protein amino acid that can be used as a building block in peptides with metal coordination ability.

scholarly journals Identification of New Ocellatin Antimicrobial Peptides by cDNA Precursor Cloning in the Frame of This Family of Intriguing Peptides

Antibiotics ◽  
2020 ◽  
Vol 9 (11) ◽  
pp. 751
Author(s):  
Mariela M. Marani ◽  
Silvana Aguilar ◽  
Ana P. Cuzziol Boccioni ◽  
Natalia L. Cancelarich ◽  
Néstor G. Basso ◽  
...  
Keyword(s):  
Antimicrobial Activity ◽  
Amino Acid ◽  
Antimicrobial Peptides ◽  
In Silico ◽  
3D Structure ◽  
Three Dimensional ◽  
Amino Acid Residues ◽  
Conserved Residues ◽  
Α Helix ◽  
In Silico Analyses

Ocellatins are a family of antimicrobial peptides found exclusively in the Leptodactylus genus. To date, 10 species have been studied and more than 23 peptides described. Here we report the sequences of five new peptides from the skin of the frog Leptodactylus latrans (Anura: Leptodactylidae) determined by cDNA cloning of the complete prepro-peptide structures. The mature peptides were characterized with in silico tools and compared with those previously described. With 21 amino acid residues, this new set of peptides not previously described in the Leptodactylus genus share between 100 and 76.2% similarity to ocellatin antimicrobial peptides. These novel peptides are cationic and their three-dimensional (3D) structure holds the highly conserved residues G1, D4, K7, and K11 and a high theoretical amphipathic α-helix content. Furthermore, in silico analyses of these new peptides predicted antimicrobial activity. This study is framed in the context of previous work published about ocellatins, and therefore, provides a review of this intriguing family of peptides.

scholarly journals Self-Assembly of Aromatic Amino Acid Enantiomers into Supramolecular Materials of High Rigidity

ACS Nano ◽  
2020 ◽  
Vol 14 (2) ◽  
pp. 1694-1706 ◽  
Author(s):  
Santu Bera ◽  
Bin Xue ◽  
Pavel Rehak ◽  
Guy Jacoby ◽  
Wei Ji ◽  
...  
Keyword(s):  
Amino Acid ◽  
Self Assembly ◽  
Aromatic Amino Acid ◽  
Supramolecular Materials ◽  
Amino Acid Enantiomers ◽  
High Rigidity

scholarly journals In VitroandIn VivoActivities of Antimicrobial Peptides Developed Using an Amino Acid-Based Activity Prediction Method

2014 ◽  
Vol 58 (9) ◽  
pp. 5342-5349 ◽  
Author(s):  
Xiaozhe Wu ◽  
Zhenling Wang ◽  
Xiaolu Li ◽  
Yingzi Fan ◽  
Gu He ◽  
...  
Keyword(s):  
Antimicrobial Activity ◽  
Amino Acid ◽  
Antimicrobial Peptides ◽  
Bacterial Load ◽  
Prediction Method ◽  
Multidrug Resistant ◽  
Antimicrobial Activities ◽  
Bacterial Strains ◽  
Content Type

ABSTRACTTo design and discover new antimicrobial peptides (AMPs) with high levels of antimicrobial activity, a number of machine-learning methods and prediction methods have been developed. Here, we present a new prediction method that can identify novel AMPs that are highly similar in sequence to known peptides but offer improved antimicrobial activity along with lower host cytotoxicity. Using previously generated AMP amino acid substitution data, we developed an amino acid activity contribution matrix that contained an activity contribution value for each amino acid in each position of the model peptide. A series of AMPs were designed with this method. After evaluating the antimicrobial activities of these novel AMPs against both Gram-positive and Gram-negative bacterial strains, DP7 was chosen for further analysis. Compared to the parent peptide HH2, this novel AMP showed broad-spectrum, improved antimicrobial activity, and in a cytotoxicity assay it showed lower toxicity against human cells. Thein vivoantimicrobial activity of DP7 was tested in aStaphylococcus aureusinfection murine model. When inoculated and treated via intraperitoneal injection, DP7 reduced the bacterial load in the peritoneal lavage solution. Electron microscope imaging and the results indicated disruption of theS. aureusouter membrane by DP7. Our new prediction method can therefore be employed to identify AMPs possessing minor amino acid differences with improved antimicrobial activities, potentially increasing the therapeutic agents available to combat multidrug-resistant infections.

Single Amino Acid Based Self-Assemblies of Cysteine and Methionine

2018 ◽  
Author(s):  
Nidhi Gour ◽  
Bharti Koshti ◽  
Chandra Kanth P. ◽  
Dhruvi Shah ◽  
Vivek Shinh Kshatriya ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Self Assembly ◽  
Aromatic Amino Acids ◽  
Neutral Condition ◽  
Single Amino Acid ◽  
Binding Assays ◽  
Human Neuroblastoma ◽  
Cytotoxicity Assays ◽  
First Time

We report for the very first time self-assembly of Cysteine and Methionine to discrenible strucutres under neutral condition. To get insights into the structure formation, thioflavin T and Congo red binding assays were done which revealed that aggregates may not have amyloid like characteristics. The nature of interactions which lead to such self-assemblies was purported by coincubating assemblies in urea and mercaptoethanol. Further interaction of aggregates with short amyloidogenic dipeptide diphenylalanine (FF) was assessed. While cysteine aggregates completely disrupted FF fibres, methionine albeit triggered fibrillation. The cytotoxicity assays of cysteine and methionine structures were performed on Human Neuroblastoma IMR-32 cells which suggested that aggregates are not cytotoxic in nature and thus, may not have amyloid like etiology. The results presented in the manuscript are striking, since to the best of our knowledge,this is the first report which demonstrates that even non-aromatic amino acids (cysteine and methionine) can undergo spontaneous self-assembly to form ordered aggregates.

Cationic Antimicrobial Peptides for Tuberculosis: A Mini-Review

2019 ◽  
Vol 20 (9) ◽  
pp. 885-892
Author(s):  
Sara Silva ◽  
Nuno Vale
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Amino Acid ◽  
Antimicrobial Peptides ◽  
Resistance Mechanisms ◽  
Therapeutic Agents ◽  
Pharmacological Properties ◽  
Therapeutic Activity ◽  
Alternative Strategies ◽  
Cationic Antimicrobial Peptides ◽  
Specific Amino Acid

Cationic antimicrobial peptides (CAMPs) can be considered as new potential therapeutic agents for Tuberculosis treatment with a specific amino acid sequence. New studies can be developed in the future to improve the pharmacological properties of CAMPs and also understand possible resistance mechanisms. This review discusses the principal properties of natural and/or synthetic CAMPs, and how these new peptides have a significant specificity for Mycobacterium tuberculosis. Also, we propose some alternative strategies to enhance the therapeutic activity of these CAMPs that include coadministration with nanoparticles and/or classic drugs.

Self-assembling behaviour of a modified aromatic amino acid in competitive medium

Soft Matter ◽  
2020 ◽  
Vol 16 (28) ◽  
pp. 6599-6607 ◽  
Author(s):  
Pijush Singh ◽  
Souvik Misra ◽  
Nayim Sepay ◽  
Sanjoy Mondal ◽  
Debes Ray ◽  
...  
Keyword(s):  
Amino Acid ◽  
Self Assembly ◽  
Aromatic Amino Acid ◽  
Photophysical Properties ◽  
Solvent Mixture ◽  
The Self ◽  
Solvent Ratio ◽  
Self Assembling

The self-assembly and photophysical properties of 4-nitrophenylalanine (4NP) are changed with the alteration of solvent and final self-assembly state of 4NP in competitive solvent mixture and are dictated by the solvent ratio.

Unique Functional Materials Derived from β-Amino Acid Oligomers

2017 ◽  
Vol 70 (2) ◽  
pp. 126 ◽  
Author(s):  
Mark P. Del Borgo ◽  
Ketav Kulkarni ◽  
Marie-Isabel Aguilar
Keyword(s):  
Amino Acid ◽  
Drug Design ◽  
Self Assembly ◽  
Functional Materials ◽  
Bioactive Molecules ◽  
Peptide Drug ◽  
New Materials ◽  
Amino Acid Oligomers

The unique structures formed by β-amino acid oligomers, or β-peptide foldamers, have been studied for almost two decades, which has led to the discovery of several distinctive structures and bioactive molecules. Recently, this area of research has expanded from conventional peptide drug design to the formation of assemblies and nanomaterials by peptide self-assembly. The unique structures formed by β-peptides give rise to a set of new materials with altered properties that differ from conventional peptide-based materials; such new materials may be useful in several bio- and nanomaterial applications.

scholarly journals Synthesis and antimicrobial activity of some novel 1,2-dihydro-[1,2,4]triazolo[1,5-a]pyrimidines bearing amino acid moiety

RSC Advances ◽  
2021 ◽  
Vol 11 (5) ◽  
pp. 2905-2916
Author(s):  
Mounir A. A. Mohamed ◽  
Adnan A. Bekhit ◽  
Omyma A. Abd Allah ◽  
Asmaa M. Kadry ◽  
Tamer M. Ibrahim ◽  
...  
Keyword(s):  
Antimicrobial Activity ◽  
Amino Acid ◽  
Green Chemistry ◽  
Antimicrobial Activities ◽  
Amino Acid Derivatives ◽  
Acid Moiety ◽  
Amino Acid Moiety

A new series of [1,2,4]-triazole bearing amino acid derivatives were synthesized under green chemistry conditions and evaluated for their antimicrobial activities.

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