PREMADE PHAGE DISPLAY LIBRARIES

Premade Phage Display Libraries

At Cell Origins, we understand that peptide and antibody discovery can be a challenge. To help overcome these challenges, we are dedicated to providing high-quality phage display libraries that are rigorously controlled to obtain the lowest rate of stop codons and other unintended sequences.

The Power of Phage Display

Phage display technology continues to play an important role in the selection and identification of peptides, monoclonal antibodies, and antibody fragments that exhibit binding affinity to specific target antigens. The technology is widely employed in the pharmaceutical industry, in which it facilitates the development of novel drugs, including peptide ligands and antibodies that target disease biomarkers. Furthermore, it is instrumental in immunology research, enabling comprehensive studies of antibody-antigen interactions. Phage display technology involves the creation of filamentous fusion phages that display random foreign peptides or antibodies on a viral coat protein. The phages are assembled into a library of peptides or antibodies, known as a phage display library.

Phage Display Using Bacteriophage Vectors

The bacteriophage vectors encode a modified version of the full phage genome that contains an antibiotic selection gene, as well as a recombinant gene encoding the foreign peptide or antibody fused to one of the coat proteins. The large size of antibodies and antibody fragments impairs the infection of E. coli and thus often leaves bacteriophage vectors unsuitable for the display of this type of ligands. However, bacteriophage vectors have been used successfully numerous times for peptide phage display on various coat proteins. Bacteriophage vectors do not require the use of helper phages for the propagation of viral particles since the phage genome contains all of the necessary genes for replication.

Phagemid-Based Phage Display

Phagemids are plasmids that contain the phage and bacterial origins of replication, and an antibiotic selection gene. Phagemids do not contain most of the wild-type genes of the filamentous phage. However, they typically encode a hybrid coat protein fused to a foreign antibody or peptide. Phagemid vectors can independently replicate in E. coli; however, they require a helper phage for the production of phage particles. The helper phage contains essential genes necessary for the assembly and release of phage clones. The smaller size of phagemid DNA enables easy transformation of E. coli, which directly relates to the diversity of the phage display library, and is, therefore, one of the most important considerations when choosing a phage display vector.

Premade Phage Display Libraries

Bacteriophage Peptide Libraries

f88-4 cys5 15-mer Cyclic>

f88-4 cys6 16-mer Cyclic>

INFO

The fUSE5 and f88-4 phage display libraries distributed by Cell origins are the original libraries created by Dr. George Smith. The diversity of these libraries have not been verified by next-generation sequencing. The diversity of each library is references from the original research articles.

The f3TR1 phage display libraries are built from the original f3TR1 vector created by Dr. George Smith. These libraries are constructed by Cell Origins and are rigorously controlled to obtain the lowest rate of stop codons and other unintended sequences. These libraries exhibit a guaranteed sequence diversity >10^10 and are accompanied by a certificate of analysis.

Linear & Cyclic Peptides

Peptides are a powerful and versatile tool offering a wide range of therapeutic and diagnostic applications. In fact, numerous peptides have successfully been used as targeting agents of various biomarkers to treat and image disease. Cyclic peptides are increasingly being used as therapeutic agents. The cyclic structure reduces peptide degradation and often results in improved binding affinity due to increased structural rigidity. Cyclic peptide libraries are thus an invaluable resource in drug discovery research.

The Success of Linear Peptides

Both linear and cyclic peptide sequences can be selected using phage display technology and each has its distinct advantages and disadvantages. Linear phage display peptide libraries have been available for decades and are typically cheaper compared to their cyclic counterparts. Additionally, the synthesis of soluble linear peptides is most often easier and more cost-effective, making them a more convenient option for researchers. However, they can have limited bioavailability due to their rapid degradation in the body, which can limit their efficacy as a drug unless they are substantially modified.

Harness the Power of Cyclic Peptides

Several novel phage display libraries of cyclic peptides have been developed over the last decade. Such phage-displayed peptide libraries are typically created by inducing disulfide bond formation between cysteine residues, or by using a scaffolding system. Cyclic peptides offer better stability due to their non-natural structure. They also typically offer higher target binding affinity and specificity as a result of their rigid structure. This makes them ideal for applications where high potency or selectivity is required.

Premade Phage Display Libraries

Linear Peptide Libraries

Cyclic Peptide Libraries

f3TR1 14-mer Cyclic>

f88-4 cys5 15-mer Cyclic>

f88-4 cys6 16-mer Cyclic>

INFO

Full-Length Antibodies & Antibody Fragments

Hybridoma technology has traditionally been used to develop monoclonal antibodies. However, phage display technology has in recent years accelerated drug discovery by assembling large Ig gene repertoires into full-length antibody libraries.

The development of antibody fragments (variable domain; Fv, single-chain variable domain; scFv, diabodies; bivalent scFvs, fragment antigen binding; Fab, and heavy-domain camelid, alpaca, llama, or shark antibody VHH fragments; nanobodies) have further advanced phage display as these are more amenable to expression compared to full-length antibodies.

Phage display libraries can be constructed from naïve or immunized donors, or designed synthetically by randomization of the complementarity-determining regions (CDR). Naïve antibody libraries typically exhibit high diversity, while libraries based on immunized donors can lead to accelerated discovery of high-affinity antibodies.

We currently do not offer premade antibody phage display libraries. However, at Cell Origins, we work with you to build a customized peptide or antibody phage display library that meets your specific goals.

Customized Libraries

Our custom libraries are made with built-in options for post-selection analysis such as biotinylation, expression of soluble ligands, affinity isolation, and more. This allows you to get the most out of your peptide or antibody phage display library and get the best results.

We provide custom solutions to create advanced peptide and antibody libraries. We customize each phage display vector to streamline your biopanning strategy and binding analyses. Our scientists work directly with you to incorporate selection and tagging strategies to make the selection of ligands with excellent binding kinetics and pharmacokinetics easier while making rapid screening assays more accurate and reliable. Our experts are here to help you every step of the way, ensuring that you get the most optimal phage display library for your needs.

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Related Products

The Vectors that Built Phage Display

In phage display technology, vectors are invaluable tools for introducing foreign genetic material into host cells, facilitating the propagation of DNA molecules, and for the production of phage virions.

Years prior to pioneering phage display technology. Dr. George P. Smith developed bacteriophage cloning vectors. Since then, the vectors have been utilized to create numerous phage display libraries of both peptides and antibodies.

Cell Origins carries the original bacteriophage vectors created by Dr. George Smith. We also offer customized bacteriophage and phagemid vectors with built-in tagging and analysis options to streamline your phage display procedures.

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Straight-Forward Library Amplification

As a leader in phage display technology, we understand the importance of amplifying stable libraries without losing ligand expression or library diversity.

Cell Origins provides E. coli strains and detailed protocols for the most optimal amplification of peptide and antibody phage display libraries.

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Easy Production of Phage Particles

Coming soon! Helper phage are required to produce phage particles when using phagemid-based vectors. Cell Origins provides helper phage and detailed protocols for straightforward amplification of phagemid peptide and antibody libraries and the production of phage particles in E. coli.

Tailored Affinity Selections for Unique Project Needs

At Cell Origins, we understand that each project is unique and requires customized protocols to meet its individual needs. We're at the forefront of utilizing phage display technology to provide exceptional biopanning services for peptide and antibody discovery.

Our customized protocols are designed to meet the unique needs of each project. We offer tailored affinity selections that begin with gaining in-depth knowledge of each target molecule or tissue to design a customized phage display biopanning protocol based on our unique multi-tiered approach. Our strategies yield proven results both in vitro and in vivo, ensuring that our clients receive quality solutions to unlock their drug discovery projects.

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Advanced Peptide and Antibody Screening

Biomolecular interactions among proteins, nucleic acids, carbohydrates, and lipids play a crucial role in biological processes. However, accurately capturing these interactions in the lab is challenging and can lead to misidentification and failure to identify hit molecules. At Cell Origins, we overcome these challenges by developing customized in vitro, in situ, or in vivo protocols for each screening procedure, ensuring the identification of the best peptides and antibodies.

At Cell Origins, we also employ our own novel approach to high-throughput screening of phage-displayed peptides and antibodies. Our novel method guarantees rapid production and purification of phage particles followed by unique biomolecular interaction analysis with 10-100x increased sensitivity compared to conventional methods.

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Published Work

Axiak-Bechtel, S. M., Leach, S. B., Scholten, D. G., Newton-Northup, J. R., Johnson, B. J., Durham, H. E., Gruber, K. A., Callahan, M. F. (2021). Pharmacokinetics and safety of TCMCB07, a melanocortin-4 antagonist peptide in dogs. Pharmacology Research & Perspectives. Vol. 9(3)

Asar, M., Franco, A., Soendergaard, M. (2020). Phage Display Selection, Identification, and Characterization of Novel Pancreatic Cancer Targeting Peptides. Biomolecules. 10(5), 714

Asar, M., Gunby, T., Franco, A., Woodson, C., Soendergaard, Mette. (2020). Identification of an Indiscriminate Peptide by Phage Display Technology. The FASEB Journal 34:1_supplement, 1-1
More

Asar, M., Newton-Northup, J., Deutscher, S., Soendergaard, M. (2019). Ovarian Cancer Targeting Phage for In Vivo Near-Infrared Optical Imaging. Diagnostics, 9, 183.

Newton-Northup, J.R., and Deutscher, S.L. (2017). Bacteriophage for the Development of Novel Tumor-Targeting Agents with Specific Pharmacokinetics and Imaging Applications. Methods in Molecular Biology in Biosensors and Biodetection.

Newton-Northup, J.R., and Deutscher, S.L.. (2016). Cytotoxic Tumor-Targeting Peptides From In Vivo Phage Display. Combinatorial Chemistry & High Throughput Screening. Vol. 19(5): 370–377

García, M. F., Zhang, X., Shah, M., Newton-Northup, J., Cabral, P., Cerecetto, H., and Quinn, T. (2016). 99mTc-bioorthogonal click chemistry reagent for in vivo pretargeted imaging. Bioorganic & Medicinal Chemistry. Vol. 24(6): 1209–1215

Newton-Northup, J.R., Dickerson, M.T., Kumar, S.R., Smith, G.P., Quinn, T.P., And Deutscher, S.L. (2014) In vivo bacteriophage peptide display to tailor pharmacokinetics of biological nanoparticles. Molecular Imaging and Biology. 16(6), 854-864.

Soendergaard M., Newton-Northup J. R., Deutscher S. L. (2014): In Vivo Phage Display Selection of an Ovarian Cancer Targeting Peptide for SPECT/CT Imaging. American Journal of Nuclear Medicine and Molecular Imaging. 4(6): 561–570.

Soendergaard, M., Newton-Northup, J.R., and Deutscher, S.L. (2014) In vitro high throughput phage display selection of ovarian cancer avid phage clones for near-infrared optical imaging. Combinatorial Chemistry and High Throughput Screening. 17(10).

Newton-Northup, J.R., and Deutscher, S.L. (2013). Contending With Target Unrelated Peptides from Phage Display. Journal of Molecular Imaging & Dynamics. Vol. 2(2):

Newton-Northup, J. R., Dickerson, M. T., Ma, L., Besch-Williford, C. L., Deutscher, S. L. (2013). Inhibition of metastatic tumor formation in vivo by a bacteriophage display-derived galectin-3 targeting peptide. Clinical & Experimental Metastasis. Vol. 30:119–132

Newton-Northup, J.R., and Deutscher, S.L. (2012) Contending with target unrelated peptides from phage display. Journal of Molecular Imaging and Dynamics. 2(2).

Soendergaard, M., Newton-Northup, J.R., Palmier, M.O., and Deutscher, S.L. (2011) Peptide phage display for discovery of novel biomarkers for imaging and therapy of cell subpopulations in ovarian cancer. Journal of Molecular Biomarkers and Diagnosis, S:2.

Newton-Northup, J.R., Figueroa, S.D., and Deutscher, S.L. (2010). Streamlined in vivo selection and screening of human prostate carcinoma avid phage particles for development of peptide based in vivo tumor imaging agents. Combinatorial chemistry & high throughput screening. 14(1):9-21

Deutscher, S. L., Dickerson, M., Gui, G., Newton, J., Holm, J. E., Vogeltanz-Holm, N., Kliethermes, B., Hewett, J. E., Kumar, S. R., Quinn, T. P., Sauter, E. R. (2010). Carbohydrate antigens in nipple aspirate fluid predict the presence of atypia and cancer in women requiring diagnostic breast biopsy. BMC Cancer. Vol. 10(519)

Newton-Northup, J.R., Figueroa, S.D., Quinn, T. P., and Deutscher, S.L. (2009). Bifunctional phage-based pretargeted imaging of human prostate carcinoma. Nuclear Medicine and Biology. Vol. 36(7):789-800

Jin, X., Newton, J. R., Montgomery, S., Smith, G. P. (2009). A generalized kinetic model for amine modification of proteins with application to phage display. Biotechniques. Vol. 46(3):175-182

Newton-Northup, J.R., and Deutscher, S.L. (2009). In vivo bacteriophage display for the discovery of novel peptide-based tumor-targeting agents. Methods in Molecular Biology. Vol. 504:275-90.

Newton-Northup, J.R., and Deutscher, S.L. (2008). Peptide Phage Display. Handbook of Experimental Pharmacology: Molecular Imaging I. Vol. 185 Pt 2:145-163.

Newton, J. R., Miao, Yubin., Deutscher, S. L., and Quinn, T. P. (2007). Melanoma Imaging with Pretargeted Bivalent Bacteriophage. Journal of Nuclear Medicine. Vol. 48(3):429-436

Newton, J. R., Kelly, K. A., Mahmood, U., Weissleder, R., and Deutscher, S. L. (2006) In vivo selection of phage for the optical imaging of PC-3 human prostate carcinoma in mice. Neoplasia. 8(9), 772-780.