Journal articles: 'Phage library'

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Farquharson, Emma L., and Sam R. Nugen. "Enterobacteria Phage Ac3's Genome Annotation and Host Range Analysis Against the ECOR Reference Library." PHAGE 3, no. 3 (September 1, 2022): 165–70. http://dx.doi.org/10.1089/phage.2022.0008.

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Petrenko, V. A., G. P. Smith, M. M. Mazooji, and T. Quinn. "α-Helically constrained phage display library." Protein Engineering, Design and Selection 15, no. 11 (November 2002): 943–50. http://dx.doi.org/10.1093/protein/15.11.943.

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Saggio, I., and R. Laufer. "Biotin binders selected from a random peptide library expressed on phage." Biochemical Journal 293, no. 3 (August 1, 1993): 613–16. http://dx.doi.org/10.1042/bj2930613.

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Recombinant biotin-binding phages were affinity-selected from a random peptide library expressed on the surface of filamentous phage. Phage binding to biotinylated proteins was half-maximally inhibited by micromolar concentrations of a monobiotinylated molecule. Sequencing of the peptide inserts of selected phages led to the identification of a previously unknown biotin-binding motif, CXWXPPF(K or R)XXC. A synthetic peptide containing this sequence motif inhibited streptavidin binding to biotinylated BSA with an IC50 of 50 microM. This compound represents the shortest non-avidin biotin-binding peptide identified to date. Our results illustrate that phage display technology can be used to identify novel ligands for a small non-proteinaceous molecule.

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Wen, Jianxin, and Kunpeng Yuan. "Phage Display Technology, Phage Display System, Antibody Library, Prospects and Challenges." Advances in Microbiology 11, no. 03 (2021): 181–89. http://dx.doi.org/10.4236/aim.2021.113013.

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Ding, Yan-Li, Mei-Yun Liu, Wei Han, Sheng-Li Yang, Hui Liu, and Yi Gong. "Application of Phage-displayed Single Chain Antibodies in Western Blot." Acta Biochimica et Biophysica Sinica 37, no. 3 (March 1, 2005): 205–9. http://dx.doi.org/10.1093/abbs/37.3.205.

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Abstract A phage display single chain fragment variable library constructed on pIII protein of M13 filamentous phage was screened using B-lymphocyte stimulator and FP248 as selective molecules. After four rounds of panning, there was a remarkable enrichment in the titer of bound phages. Twenty phage clones were selected from the last round and screened by means of phage-ELISA. With the antibody phages as primary antibodies in Western blot, we developed a method for detecting the specific antigen. The dilutions of antibody phages depend on the affinity between antibody-displayed phage particles and antigens.

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Gillespie, James W., Liping Yang, Laura Maria De Plano, Murray A. Stackhouse, and Valery A. Petrenko. "Evolution of a Landscape Phage Library in a Mouse Xenograft Model of Human Breast Cancer." Viruses 11, no. 11 (October 26, 2019): 988. http://dx.doi.org/10.3390/v11110988.

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Peptide-displayed phage libraries are billion-clone collections of diverse chimeric bacteriophage particles, decorated by genetically fused peptides built from a random combination of natural amino acids. Studying the molecular evolution of peptide-displayed libraries in mammalian model systems, using in vivo phage display techniques, can provide invaluable knowledge about the underlying physiology of the vasculature system, allow recognition of organ- and tissue-specific networks of protein–protein interactions, and provide ligands for targeted diagnostics and therapeutics. Recently, we discovered that landscape phage libraries, a specific type of multivalent peptide phage display library, expose on their surface comprehensive collections of elementary binding units (EBUs), which can form short linear motifs (SLiMs) that interact with functional domains of physiologically relevant proteins. Because of their unique structural and functional features, landscape phages can use an alternative mechanism of directed molecular evolution, i.e., combinatorial avidity selection. These discoveries fueled our interest in revisiting the in vivo evolution of phage displayed libraries using another format of display, i.e., landscape phages. In this study, we monitored the evolution of a landscape phage library in a mouse model with and without an implanted human breast cancer tumor xenograft. As expected, the multivalent architecture of landscape phage displayed proteins provided strong tissue selectivity and resulted in a huge diversity of tissue penetrating, chimeric phage particles. We identified several types of EBU interactions that evolved during the course of tissue distribution, which included interactions of EBUs with all tissue types, those EBUs that interacted selectively with specific organs or tissues with shared gene expression profiles or functionalities, and other EBUs that interacted in a tissue-selective manner. We demonstrated that landscape phage libraries are a rich collection of unique nanobioparticles that can be used to identify functional organ and tissue-binding elements after the evolution of a phage display library in vivo.

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Brichta, J., H. Vesela, and M. Franek. "Production of scFv recombinant fragments against 2,4-dichlorophenoxyacetic acid hapten using naďve phage library." Veterinární Medicína 48, No. 9 (March 30, 2012): 237–47. http://dx.doi.org/10.17221/5776-vetmed.

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Three single chain variable fragment (scFv) antibodies against 2,4-dichlophenoxyacetic acid (2,4-D) herbicide were produced by the Griffin1.library. The selection of the scFv from the phage library was carried out by 2,4-D-protein coated tubes with different levels of hapten substitution in the conjugate. The scFv phage clones were isolated within the five round library panning and the antibodies were expressed in Escherichia coli HB2151. The recombinant products were purified by metal affinity chromatography yielding 200 g of pure scFv per 1 liter of bacterial culture. The antibody fragments provided steep curves in conventional indirect ELISA having the IC<sub>50</sub> values from 10.2 to 14.5 ng/ml established for 2,4-D standard. Interestingly enough, the recombinant ScFv E1 antibody exhibited 68% cross-reactivity with 2,4-dichlorphenol (2,4-D = 100%), and 38.0% with methylchlorophenoxyacetic acid (MCPA) whereas reaction with other phenoxyacetic compounds was low. Similar characteristics were obtained for other two recombinant products. Low stability for the isolated scFv antibodies was found in storage buffer even in the presence of stabilizers and protease inhibitors. Factors influencing stability of the recombinant antibodies are discussed.

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Daniele, Sblattero, Not Tarcisio, Marzari Roberto, and Bradbury Andrew. "PHAGE ANTIBODY LIBRARY FROM CELIAC DISEASE PATIENT." Journal of Pediatric Gastroenterology & Nutrition 28, no. 5 (May 1999): 568. http://dx.doi.org/10.1097/00005176-199905000-00118.

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Barchan, D., M. Balass, M. C. Souroujon, E. Katchalski-Katzir, and S. Fuchs. "Identification of epitopes within a highly immunogenic region of acetylcholine receptor by a phage epitope library." Journal of Immunology 155, no. 9 (November 1, 1995): 4264–69. http://dx.doi.org/10.4049/jimmunol.155.9.4264.

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Abstract We have employed a hexapeptide phage-epitope library to identify epitopes for a mAb (mAb 5.14), which is directed to a determinant within a highly immunogenic, cytoplasmic region of the alpha-subunit of acetylcholine receptor (AChR). We have selected two different peptide-presenting phages (SWDDIR-phage and LWILTR-phage) which interact specifically with mAb 5.14. This interaction is specifically inhibited by AChR and by synthetic peptides corresponding to the hexapeptides presented by the selected phages. Although mAb 5.14 binds to AChR in its native as well as its denatured form, the selected hexapeptides do not exist as such in the AChR molecule. However, three amino acid sequence homologies with these hexapeptides were shown to be present in the cytoplasmic region of Torpedo AChR. By extending the selected hexapeptides, at one or both ends, with amino acid residues flanking the hexapeptides in the phage, we obtained mimotopes with an up to two order of magnitude higher affinity to the Ab. These extended peptides were able to efficiently block the binding of mAb 5.14 to both peptide-presenting phages, and to AChR.

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Duplessis, Martin, Céline M. Lévesque, and Sylvain Moineau. "Characterization of Streptococcus thermophilus Host Range Phage Mutants." Applied and Environmental Microbiology 72, no. 4 (April 2006): 3036–41. http://dx.doi.org/10.1128/aem.72.4.3036-3041.2006.

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ABSTRACT To investigate phage-host interactions in Streptococcus thermophilus, a phage-resistant derivative (SMQ-301R) was obtained by challenging a Tn917 library of phage-sensitive strain S. thermophilus SMQ-301 with virulent phage DT1. Mutants of phages DT1 and MD2 capable of infecting SMQ-301 and SMQ-301R were isolated at a frequency of 10−6. Four host range phage mutants were analyzed further and compared to the two wild-type phages. Altogether, three genes (orf15, orf17, and orf18) contained point mutations leading to amino acid substitutions and were responsible for the expanded host range. These three proteins were also identified in both phages by N-terminal sequencing and/or matrix-assisted laser desorption ionization-time-of-flight mass spectrometry. The results suggest that at least three phage structural proteins may be involved in phage-host interactions in S. thermophilus.

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Zhao, Peng, Guijie Zhu, Lihua Zhang, Zhen Liang, Zonghai Li, and Yukui Zhang. "New method for determination of average scFv fragment number displayed on the M13 phage surface." Pure and Applied Chemistry 82, no. 1 (January 3, 2010): 205–11. http://dx.doi.org/10.1351/pac-con-09-02-03.

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Single-chain-Fv (scFv) display M13 phage library has been regarded as a powerful tool for screening specific antibodies via binding with target proteins. Generally, the library quality is evaluated through detecting gene fragments by molecular biology methods, which is not only time- and labor-consuming, but also impossible to obtain quantitative information about the binding capacity of the phage library. In our recent study, a new method to calculate the average scFv number displayed on the M13 phage surface was proposed by capillary electrophoresis with laser-induced fluorescence (CE-LIF) detection. By this method, enhanced green fluorescent protein (EGFP) and scFv phage clones that could specifically bind with EGFP were mixed with different ratios, followed by analysis by CE-LIF. With the dilution of EGFP by phage solution, the peak areas of scFv phage clones and free EGFP were decreased continuously, while that of the EGFP-M13 phage complex was found to decrease initially, then trend to be stable, and finally decrease further. When the volume ratio of the M13 phage to EGFP reached 660:1, corresponding to the molecule number ratio as 1:2.6, no more EGFP was found to bind with the M13 phage, which demonstrated that, by average, 2.6 scFv fragments that could bind with EGFP were displayed on the M13 phage surface. All these experimental results demonstrated that, by such a method, the quantitative evaluation of the phage library could be achieved with high throughput and accuracy.

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Ames, R. S., M. A. Tornetta, C. S. Jones, and P. Tsui. "Isolation of neutralizing anti-C5a monoclonal antibodies from a filamentous phage monovalent Fab display library." Journal of Immunology 152, no. 9 (May 1, 1994): 4572–81. http://dx.doi.org/10.4049/jimmunol.152.9.4572.

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Abstract A panel of mAbs against the activated complement component C5a was obtained from a filamentous phage M13-Fab display library generated from mice immunized with human rC5a. Fabs isolated from the library after iterative selection vs rC5a bound to both rC5a and purified C5. To isolate Fabs specific for neoepitopes expressed on C5a but not on the native complement component C5 the library was rescreened in a competitive manner. The phage Fab library was first incubated with immobilized C5 to deplete C5 reactive Fabs. The C5 nonadherent phage were then incubated with immobilized rC5a in the presence of soluble C5. Bound phage were eluted and subjected to two additional cycles of subtraction with immobilized C5 and selection with immobilized rC5a in the presence of soluble C5. After three cycles of this competitive biopanning four Fabs reactive with rC5a were isolated. Two bound preferentially with and neutralized C5a. Competitive biopanning of phage display libraries may increase the probability of identification of Abs of the desired specificity.

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RU, BEIBEI, PETER A. C. 'T HOEN, FULEI NIE, HAO LIN, FENG-BIAO GUO, and JIAN HUANG. "PhD7FASTER: PREDICTING CLONES PROPAGATING FASTER FROM THE Ph.D.-7 PHAGE DISPLAY PEPTIDE LIBRARY." Journal of Bioinformatics and Computational Biology 12, no. 01 (January 28, 2014): 1450005. http://dx.doi.org/10.1142/s021972001450005x.

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Phage display can rapidly discover peptides binding to any given target; thus, it has been widely used in basic and applied research. Each round of panning consists of two basic processes: Selection and amplification. However, recent studies have showed that the amplification step would decrease the diversity of phage display libraries due to different propagation capacity of phage clones. This may induce phages with growth advantage rather than specific affinity to appear in the final experimental results. The peptides displayed by such phages are termed as propagation-related target-unrelated peptides (PrTUPs). They would mislead further analysis and research if not removed. In this paper, we describe PhD7Faster, an ensemble predictor based on support vector machine (SVM) for predicting clones with growth advantage from the Ph.D.-7 phage display peptide library. By using reduced dipeptide composition (ReDPC) as features, an accuracy (Acc) of 79.67% and a Matthews correlation coefficient (MCC) of 0.595 were achieved in 5-fold cross-validation. In addition, the SVM-based model was demonstrated to perform better than several representative machine learning algorithms. We anticipate that PhD7Faster can assist biologists to exclude potential PrTUPs and accelerate the finding of specific binders from the popular Ph.D.-7 library. The web server of PhD7Faster can be freely accessed at http://immunet.cn/sarotup/cgi-bin/PhD7Faster.pl .

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Bai, Xuelian, Moonseon Jang, Nam Ju Lee, Thi Thu Ha Nguyen, Mooyoung Jung, Jeong Yeon Hwang, and Hyunbo Shim. "A Novel Synthetic Antibody Library with Complementarity-Determining Region Diversities Designed for an Improved Amplification Profile." International Journal of Molecular Sciences 23, no. 11 (June 2, 2022): 6255. http://dx.doi.org/10.3390/ijms23116255.

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Antibody discovery by phage display consists of two phases, i.e., the binding phase and the amplification phase. Ideally, the selection process is dominated by the former, and all the retrieved clones are amplified equally during the latter. In reality, the amplification efficiency of antibody fragments varies widely among different sequences and, after a few rounds of phage display panning, the output repertoire often includes rapidly amplified sequences with low or no binding activity, significantly diminishing the efficiency of antibody isolation. In this work, a novel synthetic single-chain variable fragment (scFv) library with complementarity-determining region (CDR) diversities aimed at improved amplification efficiency was designed and constructed. A previously reported synthetic scFv library with low, non-combinatorial CDR diversities was panned against protein A superantigen, and the library repertoires before and after the panning were analyzed by next generation sequencing. The enrichment or depletion patterns of CDR sequences after panning served as the basis for the design of the new library. Especially for CDR-H3 with a higher and more random diversity, a machine learning method was applied to predict potential fast-amplified sequences among a simulated sequence repertoire. In a direct comparison with the previous generation library, the new library performed better against a panel of antigens in terms of the number of binders isolated, the number of unique sequences, and/or the speed of binder enrichment. Our results suggest that the amplification-centric design of sequence diversity is a valid strategy for the construction of highly functional phage display antibody libraries.

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Brigati, Jennifer, David D. Williams, Iryna B. Sorokulova, Viswaprakash Nanduri, I.-Hsuan Chen, Charles L. Turnbough, and Valery A. Petrenko. "Diagnostic Probes for Bacillus anthracis Spores Selected from a Landscape Phage Library." Clinical Chemistry 50, no. 10 (October 1, 2004): 1899–906. http://dx.doi.org/10.1373/clinchem.2004.038018.

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AbstractBackground: Recent use of Bacillus anthracis spores as a bioweapon has highlighted the need for a continuous monitoring system. Current monitoring systems rely on antibody-derived probes, which are not hardy enough to withstand long-term use under extreme conditions. We describe new, phage-derived probes that can be used as robust substitutes for antibodies.Methods: From a landscape phage library with random octapeptides displayed on all copies of the major phage coat protein of the phage fd-tet, we selected clones that bound to spores of B. anthracis (Sterne strain). ELISA, micropanning, and coprecipitation assays were used to evaluate the specificity and selectivity with which these phage bound to B. anthracis spores.Results: Peptides on the selected clones directed binding of the phage to B. anthracis spores. Most clones exhibited little or no binding to spores of distantly related Bacillus species, but some binding was observed with spores of closely related species. Our most specific spore-binding phage displayed a peptide EPRLSPHS (several thousand peptides per phage) and bound 3.5- to 70-fold better to spores of B. anthracis Sterne than to spores of other Bacillus species.Conclusions: The selected phage probes bound preferentially to B. anthracis Sterne spores compared with other Bacillus species. These phage could possibly be further developed into highly specific and robust probes suitable for long-term use in continuous monitoring devices and biosorbents.

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Song, Jiaoyang, Zhengjie Liu, Qing Zhang, Yuqing Liu, and Yibao Chen. "Phage Engineering for Targeted Multidrug-Resistant Escherichia coli." International Journal of Molecular Sciences 24, no. 3 (January 27, 2023): 2459. http://dx.doi.org/10.3390/ijms24032459.

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The lytic bacteriophages have potential application value in the treatment of bacterial infections. However, the narrow host spectrum of these phages limits their range of clinical application. Here, we demonstrate the use of scarless Cas9-assisted recombination (no-SCAR) gene-editing technology to regulate phage–host range. We used phage PHB20 as the scaffold to create agents targeting different multidrug-resistant Escherichia coli by replacing its phage tail fiber gene (ORF40). The engineered phages were polyvalent and capable of infecting both the original host bacteria and new targets. Phage-tail fiber genes can be amplified by PCR to construct a recombinant phage PHB20 library that can deal with multidrug-resistant bacteria in the future. Our results provide a better understanding of phage–host interactions, and we describe new anti-bacterial editing methods.

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Hoess, R. H., A. J. Mack, H. Walton, and T. M. Reilly. "Identification of a structural epitope by using a peptide library displayed on filamentous bacteriophage." Journal of Immunology 153, no. 2 (July 15, 1994): 724–29. http://dx.doi.org/10.4049/jimmunol.153.2.724.

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Abstract The screening of phage-displayed random peptide libraries has recently emerged as a powerful technique for probing Ab-Ag interactions. We have used this method to identify the epitope recognized by a mAb, CB5B10, raised against plasminogen activator inhibitor type-1 (PAI-1). Two phage libraries, displaying random hexapeptides with or without flanking cysteine residues, were screened for binding to mAb CB5B10. The selected phages were shown to contain similar peptide sequences, all of which were flanked by cysteines. When compared with the crystal structure of PAI-1, the selected peptides closely resemble the sequence of a solvent-exposed loop connecting the COOH-terminal of an alpha-helix at Phe114 to a beta-sheet at Ser119. Because of the constraints imposed by the flanking cysteine residues, the selected peptides appear to mimic the structure and the sequence of the PAI-1 epitope. Specific contacts between the amino acids displayed by the phage and the mAb were explored using site-directed mutants of the phage peptide. The effects of these substitutions on binding to the mAb correlated well with the accessibility of the corresponding residues in the PAI-1 epitope. This is the first example of the use of phage-displayed peptide libraries to identify a structural epitope.

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Tikunova, N. V., V. V. Morozova, T. A. Batanova, E. F. Belanov, N. I. Bormotov, and A. A. Ilyichev. "Phage antibodies from combinatorial library neutralize vaccinia virus." Human Antibodies 10, no. 3-4 (December 31, 2001): 95–99. http://dx.doi.org/10.3233/hab-2001-103-401.

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Petrenko, V. A., G. P. Smith, X. Gong, and T. Quinn. "A library of organic landscapes on filamentous phage." "Protein Engineering, Design and Selection" 9, no. 9 (1996): 797–801. http://dx.doi.org/10.1093/protein/9.9.797.

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Pini, Alessandro, Francesca Viti, Annalisa Santucci, Barbara Carnemolla, Luciano Zardi, Paolo Neri, and Dario Neri. "Design and Use of a Phage Display Library." Journal of Biological Chemistry 273, no. 34 (August 21, 1998): 21769–76. http://dx.doi.org/10.1074/jbc.273.34.21769.

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Wang, Xiaoshan Shayna, Peng‐Hsun Chase Chen, J. Trae Hampton, Jeffery M. Tharp, Catrina A. Reed, Sukant K. Das, Duen‐Shian Wang, et al. "A Genetically Encoded, Phage‐Displayed Cyclic‐Peptide Library." Angewandte Chemie International Edition 58, no. 44 (September 9, 2019): 15904–9. http://dx.doi.org/10.1002/anie.201908713.

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Wang, Xiaoshan Shayna, Peng‐Hsun Chase Chen, J. Trae Hampton, Jeffery M. Tharp, Catrina A. Reed, Sukant K. Das, Duen‐Shian Wang, et al. "A Genetically Encoded, Phage‐Displayed Cyclic‐Peptide Library." Angewandte Chemie 131, no. 44 (September 9, 2019): 16051–56. http://dx.doi.org/10.1002/ange.201908713.

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Fang, Rui, Jie Qi, Zhi-bin Lu, Hui Zhou, Wei Li, and Jiacong Shen. "Selection of Trypsin Inhibitors in Phage Peptide Library." Biochemical and Biophysical Research Communications 220, no. 1 (March 1996): 53–56. http://dx.doi.org/10.1006/bbrc.1996.0355.

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Paul, John H., Shannon J. Williamson, Amy Long, R. Nathan Authement, David John, Anca M. Segall, Forest L. Rohwer, Matthew Androlewicz, and Stacey Patterson. "Complete Genome Sequence of φHSIC, a Pseudotemperate Marine Phage of Listonella pelagia." Applied and Environmental Microbiology 71, no. 6 (June 2005): 3311–20. http://dx.doi.org/10.1128/aem.71.6.3311-3320.2005.

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ABSTRACT The genome for the marine pseudotemperate member of the Siphoviridae φHSIC has been sequenced using a combination of linker amplification library construction, restriction digest library construction, and primer walking. φHSIC enters into a pseudolysogenic relationship with its host, Listonella pelagia, characterized by sigmoidal growth curves producing >109 cells/ml and >1011 phage/ml. The genome (37,966 bp; G+C content, 44%) contained 47 putative open reading frames (ORFs), 17 of which had significant BLASTP hits in GenBank, including a β subunit of DNA polymerase III, a helicase, a helicase-like subunit of a resolvasome complex, a terminase, a tail tape measure protein, several phage-like structural proteins, and 1 ORF that may assist in host pathogenicity (an ADP ribosyltransferase). The genome was circularly permuted, with no physical ends detected by sequencing or restriction enzyme digestion analysis, and lacked a cos site. This evidence is consistent with a headful packaging mechanism similar to that of Salmonella phage P22 and Shigella phage Sf6. Because none of the phage-like ORFs were closely related to any existing phage sequences in GenBank (i.e., none more than 62% identical and most <25% identical at the amino acid level), φHSIC is unique among phages that have been sequenced to date. These results further emphasize the need to sequence phages from the marine environment, perhaps the largest reservoir of untapped genetic information.

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Sloth, Ane Beth, Babak Bakhshinejad, Malte Jensen, Camilla Stavnsbjerg, Mikkel Baldtzer Liisberg, Maria Rossing, and Andreas Kjaer. "Analysis of Compositional Bias in a Commercial Phage Display Peptide Library by Next-Generation Sequencing." Viruses 14, no. 11 (October 29, 2022): 2402. http://dx.doi.org/10.3390/v14112402.

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The principal presumption of phage display biopanning is that the naïve library contains an unbiased repertoire of peptides, and thus, the enriched variants derive from the affinity selection of an entirely random peptide pool. In the current study, we utilized deep sequencing to characterize the widely used Ph.DTM-12 phage display peptide library (New England Biolabs). The next-generation sequencing (NGS) data indicated the presence of stop codons and a high abundance of wild-type clones in the naïve library, which collectively result in a reduced effective size of the library. The analysis of the DNA sequence logo and global and position-specific frequency of amino acids demonstrated significant bias in the nucleotide and amino acid composition of the library inserts. Principal component analysis (PCA) uncovered the existence of four distinct clusters in the naïve library and the investigation of peptide frequency distribution revealed a broad range of unequal abundances for peptides. Taken together, our data provide strong evidence for the notion that the naïve library represents substantial departures from randomness at the nucleotide, amino acid, and peptide levels, though not undergoing any selective pressure for target binding. This non-uniform sequence representation arises from both the M13 phage biology and technical errors of the library construction. Our findings highlight the paramount importance of the qualitative assessment of the naïve phage display libraries prior to biopanning.

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Sawada, Toshiki, Rina Oyama, Michihiro Tanaka, and Takeshi Serizawa. "Discovery of Surfactant-Like Peptides from a Phage-Displayed Peptide Library." Viruses 12, no. 12 (December 15, 2020): 1442. http://dx.doi.org/10.3390/v12121442.

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Peptides with specific affinities for various materials have been identified in the past three decades and utilized in materials science and engineering. A peptide’s capability to specifically interact with materials is not naturally derived but screened from a biologically constructed peptide library displayed on phages or cells. To date, due to limitations in the screening procedure, the function of screened peptides has been primarily limited to the affinity for target materials. Herein, we demonstrated the screening of surfactant-like peptides from a phage-displayed peptide library. A screened phage clone displaying a peptide showed high activity for accumulating at emulsion surfaces with certain assembled structures, resulting in stable emulsions. The surface tension for the solution of the chemically synthesized peptide decreased with increasing peptide concentration, demonstrating certain surface activity, which corresponded to the ability to decrease the surface tension of liquids (e.g., water), owing to the accumulation of molecules at the air–liquid or liquid–liquid interface. Peptides with a randomized sequence did not lower the surface tension, indicating the essential role of amino acid sequences in surface activity. Our strategy for identifying novel functional peptides from a phage-displayed peptide library can be used to expand the applicability of peptidyl materials and biosurfactants.

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Ziegler, A., M. A. Mayo, and L. Torrance. "Synthetic Antigen from a Peptide Library Can Be an Effective Positive Control in Immunoassays for the Detection and Identification of Two Geminiviruses." Phytopathology® 88, no. 12 (December 1998): 1302–5. http://dx.doi.org/10.1094/phyto.1998.88.12.1302.

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Phage-displayed peptides were selected from the Cys 1 random phage display peptide library that bound strongly to the monoclonal antibody (MAb) SCR 20. The binding peptides were fused to the N-terminus of the phage protein pVIII. Preparations of the phage were shown to be effective as controls for the functionality of the SCR 20 MAb in both enzyme-linked immunosorbent assays and dot blot immunoassays. UV irradiation that eliminated phage infectivity did not greatly alter the antigenicity. Peptides displayed on phage are quick and cheap to prepare, and preparations can be standardized to ensure comparability among different assays. The peptide library approach can be readily extended for use with other MAbs to obtain inexpensive and safe standardized positive control reagents for use in immunoassays to diagnose plant disease.

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Caberoy, Nora B., Yixiong Zhou, and Wei Li. "Can Phage Display Be Used as a Tool to Functionally Identify Endogenous Eat-Me Signals in Phagocytosis?" Journal of Biomolecular Screening 14, no. 6 (June 16, 2009): 653–61. http://dx.doi.org/10.1177/1087057109335679.

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Removal of apoptotic cells and cellular debris by phagocytosis is essential for development, tissue homeostasis, and resolution of inflammation. Eat-me signals control the initiation of phagocytosis, holding a key to the understanding of phagocyte biology. Because of a lack of functional cloning strategy, eat-me signals are conventionally identified and characterized on a case-by-case basis. The feasibility of functional cloning of eat-me signals by phage display is investigated by characterizing the biological behavior of T7 phages displaying 2 well-known eat-me signals: growth arrest—specific gene 6 (Gas6) and milk fat globule—EGF8 (MFG-E8). Gas6-phage binds to all 3 known Gas6 receptors: Mer, Axl, and Tyro3 receptor tyrosine kinases. Gas6-phage and MFG-E8-phage are capable of binding to phagocytes and nonphagocytes. However, both phages stimulate phage uptake only in phagocytes, including macrophages, microglia, and retinal pigment epithelium cells, but not in nonphagocytes. Furthermore, functional phage selection by phagocytosis in phagocytes enriches both Gas6-phage and MFG-E8-phage, suggesting that phage display can be used as a tool to functionally identify unknown eat-me signals from phage display cDNA library. ( Journal of Biomolecular Screening 2009:653-661)

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Buzatti, Andréia, Arnielis Diaz Fernandez, Amilcar Arenal, Erlán Pereira, Alda Lucia Gomes Monteiro, and Marcelo Beltrão Molento. "Sheep polyclonal antibody to map Haemonchus contortus mimotopes using phage display library." Revista Brasileira de Parasitologia Veterinária 27, no. 2 (May 24, 2018): 183–90. http://dx.doi.org/10.1590/s1984-296120180023.

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Abstract The aim of this study was to evaluate phage display technology for mapping Haemonchus contortus mimotopes. We screened the PhD-7 Phage Display Peptide Library Kit with a sheep polyclonal antibody against H. contortus. After four rounds of selection, 50 phage peptide clones were selected by biopanning and sequenced. Two clones displaying peptide mimotopes of H. contortus proteins were chosen for sheep immunization: clone 6 - mimotope of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and clone 17 - mimotope of a disorganized muscle family member (Dim 1). Twelve sheep were allocated into 3 groups of 4 animals as follow: G1: control group; G2/GAPDH: immunized with clone 6; and G3/Dim1: immunized with clone 17. Four immunizations were performed at intervals of seven days (0, 7, 14, and 21 days). On day 28 post initial vaccination, all groups were orally challenged with 2500 H. contortus infective larvae. The mimotope peptides selected by phage display were recognized by IgG from sheep naturaly infected with H. contortus. The immunization protocol showed an increasein IgG anti-M13 phage titers, but no effect was observed in IgG-specific for the anti-mimotope peptides. This is the first report of successful use of a phage display library for the identification of mimotopes of H. contortus proteins.

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Fujii, Ikuo, Shiro Fukuyama, Yoshiharu Iwabuchi, and Ryuji Tanimura. "Evolving catalytic antibodies in a phage-displayed combinatorial library." Nature Biotechnology 16, no. 5 (May 1998): 463–67. http://dx.doi.org/10.1038/nbt0598-463.

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Koscielska-Kasprzak, Katarzyna, and Jacek Otlewski. "Amyloid-forming peptides selected proteolytically from phage display library." Protein Science 12, no. 8 (August 2003): 1675–85. http://dx.doi.org/10.1110/ps.0236103.

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Guo, Zhengguang, Xiaorong Wang, Huihua Li, and Youhe Gao. "Screening E3 Substrates Using a Live Phage Display Library." PLoS ONE 8, no. 10 (October 4, 2013): e76622. http://dx.doi.org/10.1371/journal.pone.0076622.

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Foti, Maria, Francesca Granucci, Paola Ricciardi-Castagnoli, Adriano Spreafico, Mathias Ackermann, and Mark Suter. "Rabbit monoclonal Fab derived from a phage display library." Journal of Immunological Methods 213, no. 2 (June 1998): 201–12. http://dx.doi.org/10.1016/s0022-1759(98)00029-5.

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Hessling, Jutta, Martin J. Lohse, and Karl-Norbert Klotz. "Peptide G protein agonists from a phage display library." Biochemical Pharmacology 65, no. 6 (March 2003): 961–67. http://dx.doi.org/10.1016/s0006-2952(02)01653-2.

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Wölcke, Julian, and Elmar Weinhold. "A DNA-BINDING PEPTIDE FROM A PHAGE DISPLAY LIBRARY." Nucleosides, Nucleotides and Nucleic Acids 20, no. 4-7 (March 31, 2001): 1239–41. http://dx.doi.org/10.1081/ncn-100002526.

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Flint, Paul W., Zhao Bo Li, Mohamed Lehar, Koichiro Saito, and Sara I. Pai. "Laryngeal Muscle Surface Receptors Identified using Random Phage Library." Laryngoscope 115, no. 11 (November 2005): 1930–37. http://dx.doi.org/10.1097/01.mlg.0000172273.98418.8d.

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Tramontano, Anna, Elisabetta Pizzi, Franco Felici, Alessandra Luzzago, Alfredo Nicosia, and Riccardo Cortese. "A database system for handling phage library-derived sequences." Gene 128, no. 1 (June 1993): 143–44. http://dx.doi.org/10.1016/0378-1119(93)90165-y.

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Zhu, Zhongyu, Yeh Ming, and Bing Sun. "Identification of Epitopes of Trichosanthin by Phage Peptide Library." Biochemical and Biophysical Research Communications 282, no. 4 (April 2001): 921–27. http://dx.doi.org/10.1006/bbrc.2001.4643.

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B., Mullaney P., Marks D. J., and Pallavicini G. M. "Mimotopes and Proteome Analyses Using Human Genomic andcDNA Epitope Phage Display." Comparative and Functional Genomics 3, no. 3 (2002): 254–63. http://dx.doi.org/10.1002/cfg.174.

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In the post-genomic era, validation of candidate gene targets frequently requires proteinbased strategies. Phage display is a powerful tool to define protein-protein interactions by generating peptide binders against target antigens. Epitope phage display libraries have the potential to enrich coding exon sequences from human genomic loci. We evaluated genomic and cDNA phage display strategies to identify genes in the 5q31 Interleukin gene cluster and to enrich cell surface receptor tyrosine kinase genes from a breast cancer cDNA library. A genomic display library containing 2 ×106clones with exon-sized inserts was selected with antibodies specific for human Interleukin-4 (IL-4) and Interleukin-13. The library was enriched significantly after two selection rounds and DNA sequencing revealed unique clones. One clone matched a cognate IL-4 epitope; however, the majority of clone insert sequences corresponded to E. coli genomic DNA. These bacterial sequences act as ‘mimotopes’ (mimetic sequences of the true epitope), correspond to open reading frames, generate displayed peptides, and compete for binding during phage selection. The specificity of these mimotopes for IL-4 was confirmed by competition ELISA. Other E. coli mimotopes were generated using additional antibodies. Mimotopes for a receptor tyrosine kinase gene were also selected using a breast cancer SKBR-3 cDNA phage display library, screened against an anti-erbB2 monoclonal antibody. Identification of mimotopes in genomic and cDNA phage libraries is essential for phage display-based protein validation assays and two-hybrid phage approaches that examine protein-protein interactions. The predominance of E. coli mimotopes suggests that the E. coli genome may be useful to generate peptide diversity biased towards protein coding sequences.Abbreviations used: IL, interleukin; ELISA, enzyme linked immunoabsorbant assay; PBS, phospho-buffered saline; cfu, colony forming units.

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Matsubara, Teruhiko, Yuko Hiura, and Katsuhiro Kawashiro. "Biocombinatorial Selection of Metal Ion-Chelating Peptides." International Journal of Modern Physics B 17, no. 08n09 (April 10, 2003): 1324–28. http://dx.doi.org/10.1142/s0217979203018946.

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A phage-displayed library selection was performed to obtain metal ion-chelating peptides. A dodecamer (12-mer) random peptide library was displayed on the surface of filamentous bacterial phage and subjected to an affinity selection. Four rounds of the selection gave fourteen Zn2+-positive phage clones. Enzyme-linked immunosorbent assay showed that the selected clones specifically bound to Zn2+ and Ni2+, but not to Cu2+ and Fe3+. Deduced amino acid sequences of the clones had histidine-rich consensus motifs. These chelating peptides should be applied to designing for metal ion-trapping biomaterials.

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Marine, Rachel, Shawn W. Polson, Jacques Ravel, Graham Hatfull, Daniel Russell, Matthew Sullivan, Fraz Syed, Michael Dumas, and K. Eric Wommack. "Evaluation of a Transposase Protocol for Rapid Generation of Shotgun High-Throughput Sequencing Libraries from Nanogram Quantities of DNA." Applied and Environmental Microbiology 77, no. 22 (September 23, 2011): 8071–79. http://dx.doi.org/10.1128/aem.05610-11.

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ABSTRACTConstruction of DNA fragment libraries for next-generation sequencing can prove challenging, especially for samples with low DNA yield. Protocols devised to circumvent the problems associated with low starting quantities of DNA can result in amplification biases that skew the distribution of genomes in metagenomic data. Moreover, sample throughput can be slow, as current library construction techniques are time-consuming. This study evaluated Nextera, a new transposon-based method that is designed for quick production of DNA fragment libraries from a small quantity of DNA. The sequence read distribution across nine phage genomes in a mock viral assemblage met predictions for six of the least-abundant phages; however, the rank order of the most abundant phages differed slightly from predictions.De novogenome assemblies from Nextera libraries provided long contigs spanning over half of the phage genome; in four cases where full-length genome sequences were available for comparison, consensus sequences were found to match over 99% of the genome with near-perfect identity. Analysis of areas of low and high sequence coverage within phage genomes indicated that GC content may influence coverage of sequences from Nextera libraries. Comparisons of phage genomes prepared using both Nextera and a standard 454 FLX Titanium library preparation protocol suggested that the coverage biases according to GC content observed within the Nextera libraries were largely attributable to bias in the Nextera protocol rather than to the 454 sequencing technology. Nevertheless, given suitable sequence coverage, the Nextera protocol produced high-quality data for genomic studies. For metagenomics analyses, effects of GC amplification bias would need to be considered; however, the library preparation standardization that Nextera provides should benefit comparative metagenomic analyses.

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Jones, Joshua D., Clare Trippett, Mehrunisha Suleman, Martha R. J. Clokie, and Jason R. Clark. "The Future of Clinical Phage Therapy in the United Kingdom." Viruses 15, no. 3 (March 10, 2023): 721. http://dx.doi.org/10.3390/v15030721.

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Bacteriophage (phage) therapy is a promising alternative antimicrobial strategy with the potential to transform the way bacterial infections are treated. In the United Kingdom, phages are classed as a biological medicine. Although no phages are licensed for UK use, they may be used as unlicensed medicinal products where licensed alternatives cannot meet a patient’s clinical needs. In the last 2 years, 12 patients in the UK have received phage therapy, and there is burgeoning clinical interest. Currently, clinical phage provision in the UK is ad hoc and relies upon networking with international sources of phages. The provision of phage therapy in the UK will not progress beyond an increasing number of ad hoc cases until an onshore sustainable and scalable source of well-characterised phages manufactured in accordance with Good Manufacturing Practice (GMP) is established. Here, we present an exciting new collaboration between UK Phage Therapy, the Centre for Phage Research at University of Leicester, CPI, and Fixed Phage. These partners, and others as we develop, will establish sustainable, scalable, and equitable phage therapy provision in the UK. We set out a vision for how phage therapy will be integrated into the NHS and healthcare more broadly, including the complementarity between licensed (cocktail) and unlicensed (personalised) phage preparations. Key elements of phage therapy infrastructure in the UK will be GMP phage manufacturing, a national phage library, and a national clinical phage centre. Together, this infrastructure will support NHS microbiology departments to develop and oversee phage therapy provision across the UK. As it will take time to deliver this, we also describe considerations for clinicians seeking to use unlicensed phage therapy in the interim. In summary, this review sets out a roadmap for the delivery of clinical phage therapy to the UK, the benefits of which we hope will reverberate for patients for decades to come.

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Tanaka, Tsuyoshi, Yoriko Kokuryu, and Tadashi Matsunaga. "Novel Method for Selection of Antimicrobial Peptides from a Phage Display Library by Use of Bacterial Magnetic Particles." Applied and Environmental Microbiology 74, no. 24 (October 24, 2008): 7600–7606. http://dx.doi.org/10.1128/aem.00162-08.

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ABSTRACT Antimicrobial peptides were isolated from a phage display peptide library using bacterial magnetic particles (BacMPs) as a solid support. The BacMPs obtained from “Magnetospirillum magneticum” strain AMB-1 consist of pure magnetite (50 to 100 nm in size) and are covered with a lipid bilayer membrane derived from the invagination of the inner membrane. BacMPs are easily purified from a culture of magnetotactic bacteria by magnetic separation. Approximately 4 × 1010 PFU of the library phage (complexity, 2.7 × 109) was reacted with BacMPs. The elution of bound phages from BacMPs was performed by disrupting its membrane with phospholipase D treatment. Six candidate peptides, which were highly cationic and could bind onto the BacMP membrane, were obtained. They exhibited antimicrobial activity against Bacillus subtilis but not against Escherichia coli and Saccharomyces cerevisiae. The amino acid substitution of the selected peptide, KPQQHNRPLRHK (peptide 6-7), to enhance the hydrophobicity resulted in obvious antimicrobial activity against all test microorganisms. The present study shows for the first time that a magnetic selection of antimicrobial peptides from the phage display peptide library was successfully achieved by targeting the actual bacterial inner membrane. This BacMP-based method could be a promising approach for a high-throughput screening of antimicrobial peptides targeting a wide range of species.

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Sun, Wei, Yan Zhang, and Zhigang Ju. "Mimotopes for Mycotoxins Diagnosis Based on Random Peptides or Recombinant Antibodies from Phage Library." Molecules 26, no. 24 (December 17, 2021): 7652. http://dx.doi.org/10.3390/molecules26247652.

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Mycotoxins, the small size secondary metabolites of fungi, have posed a threat to the safety of medicine, food and public health. Therefore, it is essential to create sensitive and effective determination of mycotoxins. Based on the special affinity between antibody and antigen, immunoassay has been proved to be a powerful technology for the detection of small analytes. However, the tedious preparation and instability of conventional antibodies restrict its application on easy and fast mycotoxins detection. By virtue of simplicity, ease of use, and lower cost, phage display library provides novel choices for antibodies or hapten conjugates, and lead random peptide or recombinant antibody to becoming the promising and environmental friendly immune-reagents in the next generation of immunoassays. This review briefly describes the latest developments on mycotoxins detection using M13 phage display, mainly focusing on the recent applications of phage display technology employed in mycotoxins detection, including the introduction of phage and phage display, the types of phage displayed peptide/recombinant antibody library, random peptides/recombinant antibodies-based immunoassays, as well as simultaneous determination of multiple mycotoxins.

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Ricca, George A., Victoria South, George H. Searfoss, Stephen French, Christopher Cheadle, Edward Murray, Richard Howk, and Michael Jaye. "Identification of Novel Peptide Antagonists for von Willebrand Factor Binding to the Platelet Glycoprotein Ib Receptor from a Phage Epitope Library." Thrombosis and Haemostasis 73, no. 01 (1995): 144–50. http://dx.doi.org/10.1055/s-0038-1653740.

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SummaryWe have constructed a fusion phage epitope library in the filamentous bacteriophage fuse5. The library was made by inserting a degenerate oligonucleotide which encodes 15 variable amino acids into the NH2-terminal region of the phage gene III protein. This library, containing over 107different epitope bearing phage, has been used in an attempt to identify inhibitors of the von Willebrand factor (vWF)-platelet Glycoprotein lb interaction. The library was screened with a monoclonal antibody (RG46) that recognizes the GPIb binding domain of vWF (amino acids 445-733). A total of 30 clones falling into 8 classes have been identified that react with the RG46 antibody. Isolates from all 8 classes are positive by immunoblot analysis. The amino acid sequence of the gene III fusion protein from positive clones showed a strong homology to the known RG46 epitope. Peptides identified from the screen were synthesized and used to demonstrate that some of the synthetic peptides exhibited inhibitory activity towards ristocetin induced binding of vWF to the GPIb receptor. Thus, we have demonstrated that screening a fusion phage epitope library with a monoclonal antibody that inhibits vWF binding to the GPIb receptor can be a useful tool not only for mapping antibody recognizing determinants, but also can serve as a source for identifying novel peptides that are antagonists for vWF binding to the platelet GPIb receptor.

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Ulrichts, H., H. Depraetere, J. Harsfalvi, and H. Deckmyn. "Selection of Phages that Inhibit vWF Interaction with Collagen under both Static and Flow Conditions." Thrombosis and Haemostasis 86, no. 08 (2001): 630–35. http://dx.doi.org/10.1055/s-0037-1616097.

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SummaryPhages from a pentadecamer phage display library were selected for binding to vWF by affinity panning. Bound phages were selectively eluted with human collagen type I. After the third round of panning 95% of individual phage clones bound to vWF. The B8-phage inhibited the binding of collagen to vWF with an IC50 of 0.6 × 1010 phages/ml, and of vWF to collagen with an IC50 of 1.0 × 1010 phages/ml at 0.5 μg/ml vWF. Under flow conditions, 1.5 × 1011 B8-phage/ml nearly completely inhibited platelet deposition on a human collagen type I coated surface at a shear rate of 1200 s-1, while phages without an insert had no effect. The peptide corresponding to the one displayed on the B8-phage competed with the phage for binding to vWF with an IC50 of 30 μg/ml (16 μM). The peptide furthermore inhibited vWF-binding to collagen with a maximum of 40% at a concentration of 1.25 mg/ml (650 μM), higher concentrations of peptide could not improve this. We thus have selected phages that are potent vWF-binders and that can be used as tools to detect vWF, to inhibit vWF-collagen interaction and to further analyse the role of vWF-collagen binding.

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Zahid, M. Shamim Hasan, T. M. Zaved Waise, M. Kamruzzaman, Amar N. Ghosh, G. Balakrish Nair, John J. Mekalanos, and Shah M. Faruque. "The Cyclic AMP (cAMP)-cAMP Receptor Protein Signaling System Mediates Resistance of Vibrio cholerae O1 Strains to Multiple Environmental Bacteriophages." Applied and Environmental Microbiology 76, no. 13 (May 14, 2010): 4233–40. http://dx.doi.org/10.1128/aem.00008-10.

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ABSTRACT Toxigenic Vibrio cholerae, the causative agent of the epidemic diarrheal disease cholera, interacts with diverse environmental bacteriophages. These interactions promote genetic diversity or cause selective enrichment of phage-resistant bacterial clones. To identify bacterial genes involved in mediating the phage-resistant phenotype, we screened a transposon insertion library of V. cholerae O1 El Tor biotype strain C6706 to identify mutants showing altered susceptibility to a panel of phages isolated from surface waters in Bangladesh. Mutants with insertion in cyaA or crp genes encoding adenylate cyclase or cyclic AMP (cAMP) receptor protein (CRP), respectively, were susceptible to a phage designated JSF9 to which the parent strain was completely resistant. Application of the cyaA mutant as an indicator strain in environmental phage monitoring enhanced phage detection, and we identified 3 additional phages to which the parent strain was resistant. Incorporation of the cyaA or crp mutations into other V. cholerae O1 strains caused similar alterations in their phage susceptibility patterns, and the susceptibility correlated with the ability of the bacteria to adsorb these phages. Our results suggest that cAMP-CRP-mediated downregulation of phage adsorption may contribute to a mechanism for the V. cholerae O1 strains to survive predation by multiple environmental phages. Furthermore, the cyaA or crp mutant strains may be used as suitable indicators in monitoring cholera phages in the water.

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Kamstrup Sell, Danna, Ane Beth Sloth, Babak Bakhshinejad, and Andreas Kjaer. "A White Plaque, Associated with Genomic Deletion, Derived from M13KE-Based Peptide Library Is Enriched in a Target-Unrelated Manner during Phage Display Biopanning Due to Propagation Advantage." International Journal of Molecular Sciences 23, no. 6 (March 18, 2022): 3308. http://dx.doi.org/10.3390/ijms23063308.

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The nonspecific enrichment of target-unrelated peptides during biopanning remains a major drawback for phage display technology. The commercial Ph.D.TM-7 phage display library is used extensively for peptide discovery. This library is based on the M13KE vector, which carries the lacZα sequence, leading to the formation of blue plaques on IPTG-X-gal agar plates. In the current study, we report the isolation of a fast-propagating white clone (displaying WSLGYTG peptide) identified through screening against a recombinant protein. Sanger sequencing demonstrated that white plaques are not contamination from environmental M13-like phages, but derive from the library itself. Whole genome sequencing revealed that the white color of the plaques results from a large 827-nucleotide genomic deletion. The phenotypic characterization of propagation capacity through plaque count- and NGS-based competitive propagation assay supported the higher propagation rate of Ph-WSLGYTG clone compared with the library. According to our data, white plaques are likely to arise endogenously in Ph.D. libraries due to mutations in the M13KE genome and should not always be viewed as exogenous contamination. Our findings also led to the conclusion that the deletion observed here might be an ancestral mutation already present in the naïve library, which causes target-unrelated nonspecific enrichment of white clone during biopanning due to propagation advantage.

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Choi, Hye Lim, Ha Rim Yang, Ha Gyeong Shin, Kyusang Hwang, Ji Woong Kim, Ji Hyun Lee, Taehoon Ryu, Yushin Jung, and Sukmook Lee. "Generation and Next-Generation Sequencing-Based Characterization of a Large Human Combinatorial Antibody Library." International Journal of Molecular Sciences 24, no. 6 (March 22, 2023): 6011. http://dx.doi.org/10.3390/ijms24066011.

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Antibody phage display is a key technology for the discovery and development of target-specific monoclonal antibodies (mAbs) for use in research, diagnostics, and therapy. The construction of a high-quality antibody library, with larger and more diverse antibody repertoires, is essential for the successful development of phage display-derived mAbs. In this study, a large human combinatorial single-chain variable fragment library (1.5 × 1011 colonies) was constructed from Epstein–Barr virus-infected human peripheral blood mononuclear cells stimulated with a combination of two of the activators of human B cells, the Toll-like receptor 7/8 agonist R848 and interleukin-2. Next-generation sequencing analysis with approximately 1.9 × 106 and 2.7 × 106 full-length sequences of heavy chain variable (VH) and κ light chain variable (Vκ) domains, respectively, revealed that the library consists of unique VH (approximately 94%) and Vκ (approximately 91%) sequences with greater diversity than germline sequences. Lastly, multiple unique mAbs with high affinity and broad cross-species reactivity could be isolated from the library against two therapeutically relevant target antigens, validating the library quality. These findings suggest that the novel antibody library we have developed may be useful for the rapid development of target-specific phage display-derived recombinant human mAbs for use in therapeutic and diagnostic applications.

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Mochizuki, Kazuto, Lisa Matsukura, Yuji Ito, Naoyuki Miyashita, and Masumi Taki. "A medium-firm drug-candidate library of cryptand-like structures on T7 phage: design and selection of a strong binder for Hsp90." Organic & Biomolecular Chemistry 19, no. 1 (2021): 146–50. http://dx.doi.org/10.1039/d0ob01855d.

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Journal articles on the topic 'Phage library'

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