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

Krumpe, Lauren R H; Mori, Toshiyuki

doi:10.1517/17460441.2.4.525

Cited by 27 publications

(15 citation statements)

References 114 publications

(122 reference statements)

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“…Peginesatide (Hematide) 1 , also a novel synthetic dimeric PEGylated erythropoietin-mimicking peptide, was designed to bind and activate the erythropoietin (EPO) receptor in order to stimulate [86,88,90,92,95,96,101,149,150].…”

Section: Phage Display Provides Leads For Therapeutic Drugsmentioning

confidence: 99%

Phage display as a technology delivering on the promise of peptide drug discovery

Hamzeh‐Mivehroud

Alizadeh

Morris

et al. 2013

Drug Discovery Today

140

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Section: Phage Display Provides Leads For Therapeutic Drugsmentioning

confidence: 99%

Phage display as a technology delivering on the promise of peptide drug discovery

Hamzeh‐Mivehroud

Alizadeh

Morris

et al. 2013

Drug Discovery Today

140

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“…While it is possible to encode a subset of amino acids with other codon schemes, there has been significant interest in using 20 trinucleotide phosphoramidites [48][49][50], thereby permitting an exact correspondence between the complexity of the DNA library and its coding potential [51]. Typically, one chooses NNK or NNS coding schemes, rather than NNN, where N is an equimolar fraction of A, C, G, or Tnucleotides, K is G or T, and S is C or G. The value of using NNK or NNS codons is that the number of oligonucleotide permutations more closely represents the number of different amino acid permutations than the NNN scheme (i.e., 32 x is closer in value to 20 x than 64 x , where x is the number of amino acids being randomized).…”

Section: Generation Of Combinatorial Peptide Librariesmentioning

confidence: 99%

“…In alanine scanning [50][51][52] (Figure 13.5), individual amino acid residues are replaced one at a time in the displayed peptide, and the impact on binding assessed in a phage enzyme-linked immunosorbent assay (ELISA, Figure 13.6). In alanine scanning [50][51][52] (Figure 13.5), individual amino acid residues are replaced one at a time in the displayed peptide, and the impact on binding assessed in a phage enzyme-linked immunosorbent assay (ELISA, Figure 13.6).…”

Section: Identifying Peptide Ligands To Protein Targetsmentioning

confidence: 99%

Phage‐Displayed Combinatorial Peptides

Huang

Pershad

Kokoszka

et al. 2011

Amino Acids, Peptides and Proteins in Organic Chemistry

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Phage-display is a convenient vehicle for the generation and screening of combinatorial peptide libraries for a variety of purposes. With standard molecular biology techniques, it is now possible to generate phage libraries displaying 10 10 different peptides, and screen them for peptide ligands to cell surfaces, metals, and proteins, or substrates of proteases, on the time frame of weeks.The first reported display of an exogenous protein fragment on the surface of bacteriophage occurred in 1985 [1]. In pioneering work by Professor George Smith, a fragment of the b-galactosidase protein of Escherichia coli was inserted into a gene encoding a minor capsid protein of M13 bacteriophage and the resulting phage were still infectious. Not only did the resulting chimeric phage particles display epitopes of the b-galactosidase protein, but also the fusion phage could be enriched more than 1000-fold over nonrecombinant phage with antibodies to the b-galactosidase protein.Protocols were subsequently developed that permitted a single fusion phage to be isolated, through affinity selection with antibodies, from an excess of 10 8 nonrecombinant phage particles [2].Combinatorial peptide libraries that were phage-displayed appeared in three simultaneous publications in 1990. In two of the publications, the linear epitopes of two different monoclonal antibodies were mapped by affinity selecting families of related peptides from libraries of 10 8 different peptides [3,4]. In the third publication, peptide ligands to streptavidin were selected from a library of 10 8 different peptides [5]. These three publications were unique in that libraries of such a large size were available for the first time and were sufficiently large enough to represent nearly all 6-mer peptide permutations. In addition, these combinatorial peptide libraries were proposed to be the source of peptide ligands to receptors, and thus serve as agonists and antagonists. Since then, phage-displayed combinatorial peptides have been the source of peptides that selectively bind cell and tissue surfaces [6-11], cytosolic proteins [12][13][14], receptors [15][16][17][18][19][20][21], inert materials [22,23], metals [24], and toxins [25][26][27].

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“…While neither of these reports was focused on cancer specific targeting, the approach is ideally suited for this application. Subsequently many papers have been published describing the isolation of tumor targeting peptides from phage displayed libraries [35, 36]. This review will focus on advances within the past 5 years in nonbiased phage display selections for the isolation of peptidic cancer targeting ligands and will highlight the novel use of these peptides in different applications.…”

Section: Introductionmentioning

confidence: 99%

Peptidic Tumor Targeting Agents: The Road from Phage Display Peptide Selections to Clinical Applications

Brown

2010

CPD

138

105

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Cancer has become the number one cause of death amongst Americans, killing approximately 1,600 people per day. Novel methods for early detection and the development of effective treatments are an eminent priority in medicine. For this reason, isolation of tumor-specific ligands is a growing area of research. Tumor-specific binding agents can be used to probe the tumor cell surface phenotype and customize treatment accordingly by conjugating the appropriate cell-targeting ligand to an anticancer drug. This refines the molecular diagnosis of the tumor and creates guided drugs that can target the tumor while sparing healthy tissues. Additionally, these targeting agents can be used as in vivo imaging agents that allow for earlier detection of tumors and micrometastasis. Phage display is a powerful technique for the isolation of peptides that bind to a particular target with high affinity and specificity. The biopanning of intact cancer cells or tumors in animals can be used to isolate peptides that bind to cancer-specific cell surface biomarkers. Over the past 10 years, unbiased biopanning of phage-displayed peptide libraries has generated a suite of cancer targeting peptidic ligands. This review discusses the recent advances in the isolation of cancer-targeting peptides by unbiased biopanning methods and highlights the use of the isolated peptides in clinical applications.

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

Cited by 27 publications

References 114 publications

Phage display as a technology delivering on the promise of peptide drug discovery

Phage display as a technology delivering on the promise of peptide drug discovery

Phage‐Displayed Combinatorial Peptides

Peptidic Tumor Targeting Agents: The Road from Phage Display Peptide Selections to Clinical Applications

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