As an undisputed forerunner and innovative explorer in the field of antibody engineering and manufacture, Creative Biolabs has established a full range of professional services based on our exclusive phage display technologies. Among of them, Creative Biolabs is proud of our outstanding M13 phage library construction service which can generate high-quality libraries for our customers all over the world.
Born in 1985, phage display is a fast, reliable and convenient method to construct large peptide libraries and offers a straightforward approach to isolate and propagate unique clones with desired properties through high efficient biopanning. This technology contributes to various research, medical and industrial applications, such as antibody discovery and engineering, epitope mapping, drug development, vaccine design, and so on. In contrast to conventional hybridoma method, phage display has demonstrated its exceptional attractiveness in the field of monoclonal antibody discovery, due to the properties of easy handling, high efficiency, diverse choices of host animals and immunogenicity independency.
Among many phage vehicles currently in apply, M13 filamentous phage has always been the most popular option and extensively used in various types of research. M13 is one template bacteriophage of E. coli with a typical long rod appearance containing a single strand DNA (6407 bp) genome. The viral coat is composed of five different capsid proteins, major capsid pVIII (2700 copies) and four minor capsids (pIII and pVI at one end while pVII and pIX at the other end). Unlike T4 and T7, M13 is lysogenic phage which is assembled in the periplasm and secreted out of the bacterial membrane without causing host lysis.
M13's multiple capsid proteins provide comprehensive display choices that can be employed to display a variety of peptides and proteins with distinctive characteristics. All five capsids have successfully exhibited foreign domain libraries, each of which makes a unique vector for different features. However, in most cases, pIII and pVIII is the preferred choices for M13 phage display.
With years of devotion and accumulation in this particular field, Creative Biolabs has been constantly developing and improving leading-edge phage display technologies while providing high-quality technical support to our worldwide clients. Based on our patent platforms and precise protocols, researchers in Creative Biolabs have successfully built up impeccable phage display libraries of diverse types (including antibody, peptide, cDNA, protein scaffold, etc.) and isolated specific clones with adequate properties. We are glad to offer these integrated services of M13 phage display libraries as well as dozens of premade antibody libraries to best facilitate our customers' research projects.
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The study focused on the development of peptide-guided lipid nanoparticles (LNPs) for the delivery of mRNA to the neural retina, aiming to treat inherited retinal degenerations. The research identified specific peptide sequences using the M13 phage display library that effectively target photoreceptors in the retina. These peptides were conjugated to LNPs, enhancing their ability to deliver mRNA to the neural retina, including photoreceptors, retinal pigment epithelium (RPE), and Müller glia, in both mice and nonhuman primates. M13 phage display library enabled the identification of retina-specific peptides that significantly improved the targeting and delivery efficiency of LNPs, making it a potential therapeutic strategy for retinal diseases. This approach represents a significant advancement in nonviral gene delivery systems for retinal therapy.
The M13 phage display library is used to study protein interactions and discover peptide sequences that can bind to specific targets, such as proteins, cells, or tissues. It involves inserting a gene encoding a peptide or protein into the M13 bacteriophage's genome. As the phage replicates, it displays the peptide on its surface. Researchers can then screen these displayed peptides for their ability to bind to a particular target, enabling the identification of high-affinity binders.
The M13 phage display library is widely used in various fields, including drug discovery, vaccine development, and diagnostics. It is particularly valuable for identifying peptides that bind specifically to disease-related proteins, which can lead to the development of therapeutic agents or diagnostic tools. Additionally, it is used in antibody engineering, allowing the selection of antibodies with high affinity for antigens.
The construction of an M13 phage display library involves inserting random peptide-encoding DNA sequences into the gene encoding the phage's coat protein, usually pIII or pVIII. This modification results in the phage displaying the encoded peptides on its surface. The library is then amplified in Escherichia coli, producing a diverse pool of phages, each displaying a different peptide, which can be screened for binding to specific targets.
The M13 phage display library has the ability to screen vast numbers of peptides, antibody fragments, or protein fragments, quickly, which increases the likelihood of identifying high-affinity binders. It also allows for the identification of fragments that can bind to targets with high specificity, even in complex biological environments. Additionally, the method is relatively inexpensive and scalable, making it accessible for a wide range of research applications.
To identify target-binding peptides, the M13 phage display library is exposed to the target of interest, such as a protein or cell surface. Phages that display peptides with high affinity for the target bind to it, while non-binding phages are washed away. The bound phages are then eluted, amplified, and subjected to additional rounds of selection to enrich for the strongest binders. The peptide sequences of the enriched phages are identified through sequencing.
In antibody engineering, the M13 phage display library is used to select antibodies with high affinity and specificity for antigens. Antibody fragments, such as single-chain variable fragments (scFvs), are displayed on the surface of the phage, and those that bind to the antigen of interest are selected. This process enables the rapid identification and optimization of antibodies for therapeutic or diagnostic use.
Biopanning is a key process in M13 phage display that involves multiple rounds of selection to enrich for phages displaying peptides with the highest affinity for a target. During each round, the phage library is incubated with the target, and non-binding phages are washed away. The bound phages are then eluted and amplified in E. coli. This process is repeated several times, with each round increasing the specificity and affinity of the selected peptides.
The M13 phage display library is used in vaccine development to identify peptide epitopes that can elicit an immune response. By selecting peptides that mimic pathogen antigens, researchers can design vaccines that stimulate the immune system to recognize and combat the actual pathogen. This method allows for the development of vaccines against diseases where traditional vaccine approaches may be less effective.
When designing an M13 phage display experiment, it is crucial to consider factors such as the diversity and quality of the phage library, the nature of the target, and the conditions of the selection process. Ensuring the target is well-presented and accessible to the phage-displayed peptides is essential for successful binding. Additionally, optimizing the washing and elution steps during biopanning is critical to select the highest affinity binders without losing potentially valuable sequences.
Use the resources in our library to help you understand your options and make critical decisions for your study.
All listed services and products are For Research Use Only. Do Not use in any diagnostic or therapeutic applications.
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