Searching Sequence Space for High-affinity Binding Peptides using Ribosome Display

Lamla, Thorsten; Erdmann, Volker A.

doi:10.1016/s0022-2836(03)00432-7

Cited by 73 publications

(64 citation statements)

References 22 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…These include synthetic one-bead-one-compound libraries [10][11][12], cell-free translation systems, such as mRNA display (peptide linked to mRNA by puromycin) [13][14][15], DNA display (DNA and peptide captured in compartments of water-in-oil emulsions) [16] and ribosome display libraries (peptide linked to mRNA by stalling the ribosome) [17][18][19], and biologic libraries, such as bacteria display [20][21][22], adenovirus display [23,24], baculovirus display [24] and bacteriophage display libraries [25][26][27][28]. GP Smith reported in 1985 that a bacteriophage could be manipulated to display foreign amino acid sequences on the surface of the phage by fusion to phage coat proteins without losing the ability of phage infectivity [28].…”

Section: Phage-displayed Peptide Library Technologymentioning

confidence: 99%

Potential of phage-displayed peptide library technology to identify functional targeting peptides

Krumpe

Mori²

2007

Expert Opinion on Drug Discovery

View full text Add to dashboard Cite

Combinatorial peptide library technology is a valuable resource for drug discovery and development. Several peptide drugs developed through phage-displayed peptide library technology are presently in clinical trials and the authors envision that phage-displayed peptide library technology will assist in the discovery and development of many more. This review attempts to compile and summarize recent literature on targeting peptides developed through peptide library technology, with special emphasis on novel peptides with targeting capacity evaluated in vivo.

show abstract

Section: Phage-displayed Peptide Library Technologymentioning

confidence: 99%

Potential of phage-displayed peptide library technology to identify functional targeting peptides

Krumpe

Mori²

2007

Expert Opinion on Drug Discovery

View full text Add to dashboard Cite

show abstract

“…Typically, a protein display method that requires in vivo gene expression is limited to a smaller library size (10 7−10 ) due to the limited capacity of bacterial transformation [6]. In contrast, larger libraries with sizes of 10 12−14 have been used in the ribosome display method [7]. Apart from that, the use of a cell-free system in ribosome display also overcomes the restrictions presented by host cells in cell-based display methods, such as the difficulty in synthesizing toxic or unstable proteins [8].…”

Section: Introductionmentioning

confidence: 99%

Photo-assisted Fabrication of Ribosome Display Microarray

Kumal¹,

Kobayashi²,

Ueno³

et al. 2014

J. Photopol. Sci. Technol.

View full text Add to dashboard Cite

Ribosome display has been widely used for in vitro protein evolution, and the formation of a ternary complex, mRNA-ribosome-protein, is central to this technology as it displays the genotype-phenotype linkage. In conventional ribosome display methods, DNA with a native sequence containing stop codons cannot be used as a starting material as the ribosome in the ternary complex is primarily stalled by the removal of stop codons. Here, a new method for ribosome display is reported. This new method enables the use of DNA containing a stop codon as a starting material and presents the ribosome display on a microarray format with the assistance of a photo-crosslinker. This method is expected to be more advantageous than the conventional method as it allows the use of DNA with a native sequence without any modification, and since it is presented on a microarray format, it enables immediate functional identification and comparison between different proteins without any downstream processing.

show abstract

“…Therefore, the complexities of libraries are limited by transformation efficiency to about 10 9 sequences. This limitation could be resolved for in vitro display technologies such as ribosome displays (19,23,24,26,27,28,29,32) by introducing a cell-free translation system. Since this system does not require transformation, large libraries can be prepared and utilized for selection.…”

mentioning

confidence: 99%

Functional Selection of Hepatitis C Virus Envelope E2-Binding Peptide Ligands by Using Ribosome Display

Chen

Zhao

Liu

et al. 2010

Antimicrob Agents Chemother

View full text Add to dashboard Cite

Small peptides that inhibit the hepatitis C virus (HCV) at the stage of viral entry have the potential to serve as attractive antiviral drugs. Ribosome display is a cell-free system for in vitro selection of peptides from large random peptide libraries. Thus, we utilized a ribosome display library technique for affinity selection of HCV envelope protein E2-binding peptide ligands. Through 13 rounds of selection, the ribosome display system generated high-affinity 12-mer peptides, and the selected peptide PE2D (MAR HRNWPLVMV) demonstrated the highest specificity and affinity to the HCV E2 protein. Furthermore, amino acids 489 to 508 (YPPRPCGIVPAKSVCGPVYC) of E2 were identified as crucial for binding to PE2D. The selected peptides, especially PE2D, not only dramatically blocked E2 protein binding to hepatocytes but also dramatically inhibited HCV cell culture (HCVcc) entry into hepatocytes. HCVcc and HCV particles from HCV patient serum samples could also be specifically captured using PE2D. Our study demonstrates that the newly selected peptide ligand PE2D holds great promise for developing a new molecular probe, a therapeutic drug specifically for HCV, or an early-diagnostic reagent for HCV surface envelope antigen E2.Hepatitis C virus (HCV) is a major cause of chronic liver disease worldwide, and infection with this virus frequently results in cirrhosis and hepatocellular carcinoma (6, 9). Humans and chimpanzees are the only species that are susceptible to HCV infection. The lack of a small-animal model and difficulties in propagating HCV in cell culture have hampered HCV research. However, the production of infectious HCV in tissue culture was recently established from a cloned JFH-1 viral genome and has since been widely applied in many labs around the world (35,51,60). This new technique has played an important role in HCV-related research and drug discovery.

show abstract

Searching Sequence Space for High-affinity Binding Peptides using Ribosome Display

Cited by 73 publications

References 22 publications

Potential of phage-displayed peptide library technology to identify functional targeting peptides

Potential of phage-displayed peptide library technology to identify functional targeting peptides

Photo-assisted Fabrication of Ribosome Display Microarray

Functional Selection of Hepatitis C Virus Envelope E2-Binding Peptide Ligands by Using Ribosome Display

Contact Info

Product

Resources

About