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Research and Application of Antibacterial Peptides in Medicine Science

Antibacterial Peptides in Medicine Science

Background Knowledge 

There are various pathogenic microorganisms in nature that seriously affect human health and survival, and the usual method of combating pathogenic microorganisms is through the use of antibiotics. Although this approach is simple and convenient, it can easily lead to increased bacterial resistance and is often difficult to effectively eliminate.

The problems of abuse, drug resistance, side effects, and residues caused by the use of antibiotics have become major challenges that plague human health and development. Finding efficient, broad-spectrum, residue free, drug resistant, and low side effect antibiotic substitutes has been a goal that people have been striving for in recent years.

New Generation Antibiotic Substitutes: Antibacterial Peptides

According to research from Omizzur Peptide (a lab focused on peptide synthesis and research), on the self evolution of multicellular organisms, the invasion of pathogenic microorganisms into the organism produces a series of protective mechanisms, one of which is the production of antibacterial substances to effectively control various pathogenic microorganisms, and antimicrobial peptides are one of the important antibacterial substances.

Antibacterial peptides have the potential to become a new generation of antibiotic substitutes due to their unique properties and antibacterial mechanisms. Antibacterial peptides have unique structural sequences, mechanisms of action, and efficient bactericidal effects, making them different from traditional antibiotic substitutes and less prone to drug resistance. At the same time, they do not have cross resistance with traditional antibiotics, and have broad application prospects.

Classification of the Origin and Mechanism of Action of Antibacterial Peptides

Antibacterial peptide is an alkaline peptide with antibacterial activity discovered by Swedish scientist Boman in Escherichia coli cells in 1974. This substance with antibacterial activity was officially named cecropin 1981.

According to existing multiple experimental results, it can be shown that most antimicrobial peptides can directly act on microbial cell membranes. The most basic mechanism of action of most antimicrobial peptides is that due to the positive charge of the peptides, they bind to the negatively charged phospholipid membrane through electrostatic action, forming a spiral or folded structure, which in turn forms ion channels on the cell membrane or lyses the cell membrane, ultimately damaging the structure of the cell or bacterial plasma membrane, causing a large amount of water-soluble substances to seep out, thereby achieving the effect of killing the target microorganisms.

Recent research has proposed new perspectives on the mechanism of action of antimicrobial peptides. Some studies have found that some antimicrobial peptides first attract and bind to the cell membrane through electrostatic interactions, and the ion channels formed are instantaneous. It can cause antimicrobial peptides to enter the cytoplasm and interact with cellular contents, such as inhibiting nucleotides, inhibiting proteins, and affecting mitochondria.

Due to the safe and effective antibacterial functions of antimicrobial peptides themselves, and the structural characteristics of their molecules being an important basis for exerting the aforementioned mechanisms, artificial modification and synthesis of antimicrobial peptides have important significance.

Chemical Structure of Antimicrobial Peptides

Antibacterial peptides are small molecule peptides with biological activity, with a molecular weight of around 2-7KD (less than 70 amino acids). They exist in all organisms and are the main cornerstone of the innate immune system that protects the host from infection. They play multiple functions in the biological system.

Antibacterial peptides have broad-spectrum antibacterial activity and have been proven to have some of the effects of traditional antibiotics. Due to the unique antibacterial mechanism of antimicrobial peptides, they can quickly kill bacteria and are less prone to developing drug resistance.

Artificial Synthesis Method of Antibacterial Peptides

The main sources of antimicrobial peptides usually come from the following three pathways: extraction and purification from organisms, chemical synthesis, and construction of genetically engineered strains of antimicrobial peptides. The latter two methods are generally used for artificial synthesis of antimicrobial peptides.

1. Chemical Synthesis Methods

Due to the short amino acid composition chains of some antimicrobial peptides, chemical synthesis methods can be more convenient to synthesize antimicrobial peptides that are completely identical in structure and function to natural antimicrobial peptides.

Nowadays, the main application in the synthesis of active antimicrobial peptides is through the combination of solid-phase synthesis technology of peptides and combinatorial chemistry technology.

2. Genetic engineering synthesis of antimicrobial peptides

Chemically synthesized antimicrobial peptides have certain constraints due to their cost and other factors. In addition to chemical methods, genetic engineering antimicrobial peptides are also feasible ways to replace natural antimicrobial peptides in theory and practice.

The development of new instruments and the improvement of synthesis technology have led to the rapid development of genetic engineering. The large-scale preparation and production of anti peptide also have certain conditions. Currently, synthetic instruments can synthesize nucleotide sequence fragments with a length of over 100 bp, providing an important way to obtain the target gene.

There are two common expression systems for antimicrobial peptides: eukaryotic and prokaryotic. In the prokaryotic expression system, the Escherichia coli expression system is representative; The yeast expression system is currently the most commonly used in eukaryotic expression systems and is the main representative of eukaryotic expression systems.

FAQs: Common Issues With Synthetic Antimicrobial Peptides

1. What are the problems with synthesizing antimicrobial peptides using chemical synthesis methods?

For shorter gene sequences synthesized through chemical synthesis, due to the usually small size of antimicrobial peptide molecules, the generated antimicrobial peptides have similar biological activity to natural antimicrobial peptides, and their design can also avoid the chance of incorrect pairing caused by PCR methods. Therefore, chemical synthesis is a commonly used method.

However, chemical synthesis has certain limitations on the length of peptide synthesis due to material costs and technological reasons, and often requires a longer time, which limits the development and application of new antibacterial peptides.

2. What are the problems with the genetic engineering expression of antimicrobial peptides?

The current problems in gene engineering expression of antimicrobial peptides can be summarized as follows: antimicrobial peptide molecules are small, easily degraded by proteases, and have stability issues; Lack of methods for detecting antimicrobial peptides.

Although genetically engineered antimicrobial peptides are consistent with natural antimicrobial peptides in their primary structure, they cannot guarantee complete consistency in their spatial structure, which may lead to differences in activity between the two.

Some antimicrobial peptides have a wide antibacterial spectrum and strong killing power, resulting in certain cytotoxicity. The generated expression products may have a certain inhibitory effect on the host, and even cause corresponding harm.

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