Recognition of cell-specific binding of phage display derived peptides using an acoustic wave sensor

Samoylov, Alexandre M.; Samoylova, Tatiana I.; Hartell, Mark G.; Pathirana, Suram; Smith, B. F.; Vodyanoy, Vitaly

doi:10.1016/s1389-0344(01)00108-3

Cited by 19 publications

(11 citation statements)

References 6 publications

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“…We therefore genetically inserted the muscle-targeting peptide ASSLNIA26,27 after 587 or 588 site of the AAV2 capsid gene, resulting two MTP-modified AAV2 capsid mutants: AAV 587 MTP and AAV 588 MTP (Fig. 1a).…”

Section: Resultsmentioning

confidence: 99%

“…In this report we describe the construction and evaluation of AAV2 vectors genetically modified with a muscle-targeting peptide (MTP), which was originally isolated by phage display in differentiated muscle cells in vitro and muscle tissue in vivo 26,27. The MTP-modified AAV2 showed improved tropisms to the striated muscles, and could efficiently and selectively infect differentiated muscle cells in vitro and skeletal and cardiac muscles in vivo .…”

Section: Introductionmentioning

confidence: 99%

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A muscle-targeting peptide displayed on AAV2 improves muscle tropism on systemic delivery

Yuan

Cao

et al. 2009

Gene Ther

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Adeno-associated virus (AAV) has become a leading gene transfer vector for striated muscles. However, the AAV vectors also exhibit broad tropisms after systemic delivery. In an attempt to improve muscle tropism, we inserted a 7-amino-acid (ASSLNIA) muscle-targeting peptide (MTP) in the capsids of AAV2 at residue 587 or 588, generating AAV587MTP and AAV588MTP. In vitro studies showed that both viruses diminished their infectivity on non-muscle cell lines as well as on un-differentiated myoblasts, however, preserved or enhanced their infectivity on differentiated myotubes. AAV587MTP, but not AAV588MTP, also abolished its heparin-binding capacity and infected myotubes in a heparin-independent manner. Furthermore, in vivo studies by intravenous vector administration in mice showed that AAV587MTP enhanced its tropism to various muscles and particularly to the heart (24.3 fold of unmodified AAV2), whereas reduced its tropism to the non-muscle tissues such as the liver, lungs and spleen, etc. This alteration of tissue tropism is not simply due to the loss of heparin-binding, since a mutant AAV2 (AAVHBSMut) containing heparin-binding site mutations lost infectivity on both non-muscle and muscle cells. Furthermore, free MTP peptide, but not the scrambled control peptide, competitively inhibited AAV587MTP infection on myotubes. These results suggest that AAV2 could be re-targeted to the striated muscles by a muscle-targeting peptide inserted after residue 587 of the capsids. This proof of principle study showed first evidence of peptide-directed muscle targeting upon systemic administration of AAV vectors.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

A muscle-targeting peptide displayed on AAV2 improves muscle tropism on systemic delivery

Yuan

Cao

et al. 2009

Gene Ther

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“…Traditionally, phage specificity and selectivity are quantified by titering of cell-associated phage [124,114] which is a time consuming method, but much more sensitive for this application. Recently, to determine peptide ligand selectivity and specificity, we developed an innovative approach based on peptide biosensors [125]. The approach allows the detection of cell surface cross-species markers in tissue homogenates, and can be used for cell suspensions as well [126].…”

Section: Targeting Of Glioma With Peptide/antibody Ligands Identifiedmentioning

confidence: 99%

Molecular Markers of Glial Tumors: Current Targeting Strategies

Samoylova

Morrison²,

Cox³

2003

CMC

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Diagnosis and therapy for malignant gliomas represents one of the most challenging problems in clinical oncology. Current treatment of malignant glioma is multimodal, involving surgical resection, radiotherapy and chemotherapy. Even with these combined therapies, patients usually die within 1 to 2 years after onset of symptoms. Clearly, improved strategies for selective delivery of therapeutic agents to gliomas are needed to combat these devastating and usually fatal cancers. This review summarizes current knowledge concerning targetable molecular markers on the surface of glial tumor cells and tumor vasculature. Such markers are altered or up-regulated in gliomas compared to normal tissues, or they might be glioma-restricted. These markers include growth factor receptors, cell-surface adhesion molecules, and membrane-type matrix metalloproteinases. Current approaches that utilize growth factor peptides and peptide/antibodies identified via phage display technology as carrier ligands for targeting malignant gliomas are discussed.

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“…[23][24][25][26][27][28] In addition, it manifests concentration dependent enzymatic activation by landscape phage derived antibody peptides. [29][30][31][32][33][34][35] These findings, GAL's commercial availability, and the technical ease of its ELISA 36,37 encouraged its selection as the target globular protein.…”

Section: Introductionmentioning

confidence: 99%

Designing allosteric peptide ligands targeting a globular protein

et al. 2006

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Patented signal analytic algorithms applied to hydrophobically transformed, numerical amino acid sequences have previously been used to design short, protein‐targeted, L or D retro‐inverso peptides. These peptides have demonstrated allosteric and/or indirect agonist effects on a variety of G‐protein and tyrosine kinase coupled membrane receptors with 30% to over 80% hit rates. Here we extend these approaches to a globular protein target. We designed eight peptide ligands targeting an ELISA antibody responsive protein, β‐galactosidase, βGAL. Three of the eight 14mer peptides allosterically activated βGAL with ELISA methodology. Using Bayesian statistics, this 38% hit rate would have occurred 2 × 10−9 by chance. These peptides demonstrated binding site competitive or noncompetitive interactions, suggesting allosteric site multiplicity with respect to their βGAL binding‐mediated ELISA signal. Kinetic studies demonstrated the temperature dependence of the βGAL peptide binding functions. Using the van't Hoff relation, we found evidence for enthalpy–entropy compensation. This relation is often found for hydrophobic interactions in aqueous media, and is consistent with the postulated hydrophobic series encoding underlying our protein‐targeted, peptide design methods. It appears that our algorithmic, hydrophobic autocovariance eigenvector template approach to the design of allosteric peptides targeting membrane receptors may also be applicable to the design of peptide ligands targeting nonmembrane involved globular proteins. © 2006 Wiley Periodicals, Inc. Biopolymers 85: 38–59, 2007.This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com

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Recognition of cell-specific binding of phage display derived peptides using an acoustic wave sensor

Cited by 19 publications

References 6 publications

A muscle-targeting peptide displayed on AAV2 improves muscle tropism on systemic delivery

A muscle-targeting peptide displayed on AAV2 improves muscle tropism on systemic delivery

Molecular Markers of Glial Tumors: Current Targeting Strategies

Designing allosteric peptide ligands targeting a globular protein

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