scholarly journals The antimicrobial peptide database provides a platform for decoding the design principles of naturally occurring antimicrobial peptides

2019 ◽  
Vol 29 (1) ◽  
pp. 8-18 ◽  
Author(s):  
Guangshun Wang
Keyword(s):  
Antimicrobial Peptides ◽  
Antimicrobial Peptide ◽  
Design Principles ◽  
Naturally Occurring ◽  
Peptide Database

Antimicrobial peptide database helps design novel antimicrobial peptides

Toxicon ◽  
2019 ◽  
Vol 158 ◽  
pp. S76
Author(s):  
Zhipeng Xie ◽  
Manchuriga Wang ◽  
Yingxia Zhang
Keyword(s):  
Antimicrobial Peptides ◽  
Antimicrobial Peptide ◽  
Peptide Database

Antimicrobial activity and membrane interaction mechanism of the antimicrobial peptides derived from Rana chensinensis with short sequences

Biologia ◽  
2017 ◽  
Vol 72 (9) ◽  
Author(s):  
Min Shen ◽  
Weibing Dong ◽  
Jun Qian ◽  
Li Zou
Keyword(s):  
Antimicrobial Activity ◽  
Antimicrobial Peptides ◽  
Bacterial Infection ◽  
Antimicrobial Peptide ◽  
Therapeutic Agent ◽  
Interaction Mechanism ◽  
Membrane Interaction ◽  
Rana Chensinensis ◽  
Potential Therapeutic Agent ◽  
Naturally Occurring

AbstractThe antimicrobial peptide chensinin-1b is a potential therapeutic agent against bacterial infection, which was derived from chensinin-1, a naturally occurring antimicrobial peptide derived from Chinese brown frog

The Modification and Design of Antimicrobial Peptide

2018 ◽  
Vol 24 (8) ◽  
pp. 904-910 ◽  
Author(s):  
Yidan Gao ◽  
Hengtong Fang ◽  
Lu Fang ◽  
Dawei Liu ◽  
Jinsong Liu ◽  
...  
Keyword(s):  
Chemical Modification ◽  
Antimicrobial Peptide ◽  
Protein Modification ◽  
Recent Progress ◽  
Therapeutic Agents ◽  
Manufacturing Cost ◽  
Commercial Development ◽  
Biochemical Modification ◽  
Naturally Occurring ◽  
Application Prospects

The antimicrobial peptides (AMPs) are a group of unique naturally occurring anti-microbial compounds with around 50 amino acids. It represents promising therapeutic agents to the infectious disease without concerning about drug resistance. However, commercial development of these peptides for even the simplest application has been hindered by the limitations of sources, instability, toxicity and bioavailability. To improve the properties of the artificial synthesized AMPs, the modification and design are the hotspots of the AMPs research. In fact, more than half of the known AMPs are naturally modified. In this review, two types of modification strategies, biochemical modification and chemical modification were summarized. Although, the chemical modification is versatile and direct, the manufacturing cost is greatly increased compared to the antibiotics. With the recent progress of the protein modification enzyme, the biochemical modification of the antimicrobial peptide followed by heterologous expression has great application prospects.

Antimicrobial Peptides: A Promising Avenue for Human Healthcare

2020 ◽  
Vol 21 (2) ◽  
pp. 90-96 ◽  
Author(s):  
Girish M. Bhopale
Keyword(s):  
Antimicrobial Peptides ◽  
Antimicrobial Peptide ◽  
Antimicrobial Agents ◽  
Current Status ◽  
Antimicrobial Drugs ◽  
Spectrum Activity ◽  
Low Levels ◽  
Human Healthcare ◽  
Broad Spectrum Activity ◽  
Promising Avenue

Antimicrobial drugs resistant microbes have been observed worldwide and therefore alternative development of antimicrobial peptides has gained interest in human healthcare. Enormous progress has been made in the development of antimicrobial peptide during the last decade due to major advantages of AMPs such as broad-spectrum activity and low levels of induced resistance over the current antimicrobial agents. This review briefly provides various categories of AMP, their physicochemical properties and mechanism of action which governs their penetration into microbial cell. Further, the recent information on current status of antimicrobial peptide development, their applications and perspective in human healthcare are also described.

scholarly journals A mixed chirality α-helix in a stapled bicyclic and a linear antimicrobial peptide revealed by X-ray crystallography

2021 ◽  
Author(s):  
Stéphane Baeriswyl ◽  
Hippolyte Personne ◽  
Ivan Di Bonaventura ◽  
Thilo Köhler ◽  
Christian van Delden ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Antimicrobial Peptide ◽  
Crystal Structures ◽  
X Ray ◽  
X Ray Crystallography ◽  
Α Helix

We report the first X-ray crystal structures of mixed chirality α-helices comprising only natural residues as the example of bicyclic and linear membrane disruptive amphiphilic antimicrobial peptides containing seven l- and four d-residues.

scholarly journals Expression of Anti-Lipopolysaccharide Factor Isoform 3 in Chlamydomonas reinhardtii Showing High Antimicrobial Activity

Marine Drugs ◽  
2021 ◽  
Vol 19 (5) ◽  
pp. 239
Author(s):  
Anguo Li ◽  
Ruihao Huang ◽  
Chaogang Wang ◽  
Qunju Hu ◽  
Hui Li ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Antimicrobial Peptide ◽  
Chlamydomonas Reinhardtii ◽  
Penaeus Monodon ◽  
Total Soluble Protein ◽  
Cell Factory ◽  
Gram Positive Bacteria ◽  
Resistance Selection ◽  
Expression Cluster ◽  
Potential Strategy

Antimicrobial peptides are a class of proteins with antibacterial functions. In this study, the anti-lipopolysaccharide factor isoform 3 gene (ALFPm3), encoding an antimicrobial peptide from Penaeus monodon with a super activity was expressed in Chlamydomonas reinhardtii, which would develop a microalga strain that can be used for the antimicrobial peptide production. To construct the expression cluster, namely pH2A-Pm3, the codon optimized ALFPm3 gene was fused with the ble reporter by 2A peptide and inserted into pH124 vector. The glass-bead method was performed to transform pH2A-Pm3 into C. reinhardtii CC-849. In addition to 8 μg/mL zeocin resistance selection, the C. reinhardtii transformants were further confirmed by genomic PCR and RT-PCR. Western blot analysis showed that the C. reinhardtii-derived ALFPm3 (cALFPm3) was successfully expressed in C. reinhardtii transformants and accounted for 0.35% of the total soluble protein (TSP). Furthermore, the results of antibacterial assay revealed that the cALFPm3 could significantly inhibit the growth of a variety of bacteria, including both Gram-negative bacteria and Gram-positive bacteria at a concentration of 0.77 μM. Especially, the inhibition could last longer than 24 h, which performed better than ampicillin. Hence, this study successfully developed a transgenic C. reinhardtii strain, which can produce the active ALFPm3 driven from P. monodon, providing a potential strategy to use C. reinhardtii as the cell factory to produce antimicrobial peptides.

scholarly journals Beneficial Impacts of Incorporating the Non-Natural Amino Acid Azulenyl-Alanine into the Trp-Rich Antimicrobial Peptide buCATHL4B

Biomolecules ◽  
2021 ◽  
Vol 11 (3) ◽  
pp. 421
Author(s):  
Areetha R. D’Souza ◽  
Matthew R. Necelis ◽  
Alona Kulesha ◽  
Gregory A. Caputo ◽  
Olga V. Makhlynets
Keyword(s):  
Amino Acid ◽  
Antimicrobial Peptides ◽  
Antimicrobial Peptide ◽  
Mechanism Of Action ◽  
Bactericidal Activity ◽  
Antimicrobial Agents ◽  
Human Cells ◽  
Side Chains ◽  
Natural Amino Acid ◽  
Proteolytic Stability

Antimicrobial peptides (AMPs) present a promising scaffold for the development of potent antimicrobial agents. Substitution of tryptophan by non-natural amino acid Azulenyl-Alanine (AzAla) would allow studying the mechanism of action of AMPs by using unique properties of this amino acid, such as ability to be excited separately from tryptophan in a multi-Trp AMPs and environmental insensitivity. In this work, we investigate the effect of Trp→AzAla substitution in antimicrobial peptide buCATHL4B (contains three Trp side chains). We found that antimicrobial and bactericidal activity of the original peptide was preserved, while cytocompatibility with human cells and proteolytic stability was improved. We envision that AzAla will find applications as a tool for studies of the mechanism of action of AMPs. In addition, incorporation of this non-natural amino acid into AMP sequences could enhance their application properties.

Prokaryotic selectivity and LPS-neutralizing activity of short antimicrobial peptides designed from the human antimicrobial peptide LL-37

Peptides ◽  
2012 ◽  
Vol 35 (2) ◽  
pp. 239-247 ◽  
Author(s):  
Yong Hai Nan ◽  
Jeong-Kyu Bang ◽  
Binu Jacob ◽  
Il-Seon Park ◽  
Song Yub Shin
Keyword(s):  
Antimicrobial Peptides ◽  
Antimicrobial Peptide ◽  
Neutralizing Activity

The evolution of the antimicrobial peptide database ( APD ) over 18 years: Milestones and new features

2021 ◽  
Author(s):  
Guangshun Wang ◽  
C. Michael Zietz ◽  
Ashok Madgapalli ◽  
Shuona Wang ◽  
Zhe Wang
Keyword(s):  
Antimicrobial Peptide ◽  
Peptide Database

scholarly journals Modulation of Human Complement System by Antimicrobial Peptide Arenicin-1 from Arenicola marina

Marine Drugs ◽  
2018 ◽  
Vol 16 (12) ◽  
pp. 480 ◽  
Author(s):  
Ekaterina Umnyakova ◽  
Nikolay Gorbunov ◽  
Alexander Zhakhov ◽  
Ilia Krenev ◽  
Tatiana Ovchinnikova ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Antimicrobial Peptide ◽  
Complement System ◽  
Complement Activation ◽  
Marine Invertebrates ◽  
Cytotoxic Agents ◽  
Arenicola Marina ◽  
Low Concentrations ◽  
Marine Polychaete ◽  
Hypothetical Mechanism

Antimicrobial peptides from marine invertebrates are known not only to act like cytotoxic agents, but they also can display some additional activities in mammalian organisms. In particular, these peptides can modulate the complement system as was described for tachyplesin, a peptide from the horseshoe crab. In this work, we investigated the influence on complement activation of the antimicrobial peptide arenicin-1 from the marine polychaete Arenicola marina. To study effects of arenicin on complement activation in human blood serum, we used hemolytic assays of two types, with antibody sensitized sheep erythrocytes and rabbit erythrocytes. Complement activation was also assessed, by the level of C3a production that was measured by ELISA. We found that the effect of arenicin depends on its concentration. At relatively low concentrations the peptide stimulates complement activation and lysis of target erythrocytes, whereas at higher concentrations arenicin acts as a complement inhibitor. A hypothetical mechanism of peptide action is proposed, suggesting its interaction with two complement proteins, C1q and C3. The results lead to the possibility of the development of new approaches for therapy of diseases connected with complement dysregulation, using peptide regulators derived from natural antimicrobial peptides of invertebrates.

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