Abstract
This review focuses on the application of two classes of peptides, i.e., self-assembling peptides (SAPs) and cell-targeting peptides (CTPs), in the development of nanocarrier delivery systems. Self-assembling peptides are emerging in a wide range of biomedical and bioengineering applications and fall into several classes, including peptide amphiphilies, bolaamphiphile peptides, cyclic peptides, and ionic complementary peptides, which can be found naturally or synthesized. The advantage of synthesizing peptides is that their self-assembling properties can be exploited to form desirable structures for various applications. Another, unique property of self-assembling peptides, is stimuli-responsibility in different environments including various pHs, temperatures, ionic strengths, etc. These characteristics make peptides applicable in a wide range of biomaterials in drug discovery. This study reviews the design principles of well-known selfassembling peptides, as well as their physical/chemical properties. In addition, it discusses the therapeutic cancer-targeting peptides and current combinatorial peptide library methods used to identify targeting peptides. Cancer-targeting peptides can target either tumor cell surfaces or tumor vasculature. The RGD peptide is one of the first tumor-targeting peptides that can bind to self-assembling peptides or any other nanocarrier to improve the therapeutic efficiency of targeting drug delivery systems.
Keywords: Cell-targeting peptide, combinatorial peptide library, ionic-complementary, phage-display, self-assembling peptide, stimuli-responsive, tumor targeting, vasculature, therapeutic cancer-targeting peptides, therapeutic efficiency, drug delivery systems, nanocarrier delivery systems, metastases, nanotechnology, bolaamphiphile peptides
Current Pharmaceutical Biotechnology
Title: Self-Assembling Peptides: Potential Role in Tumor Targeting
Volume: 12 Issue: 8
Author(s): Parisa Sadatmousavi, M. Soltani, Reyhaneh Nazarian, Mousa Jafari and P. Chen
Affiliation:
Keywords: Cell-targeting peptide, combinatorial peptide library, ionic-complementary, phage-display, self-assembling peptide, stimuli-responsive, tumor targeting, vasculature, therapeutic cancer-targeting peptides, therapeutic efficiency, drug delivery systems, nanocarrier delivery systems, metastases, nanotechnology, bolaamphiphile peptides
Abstract: This review focuses on the application of two classes of peptides, i.e., self-assembling peptides (SAPs) and cell-targeting peptides (CTPs), in the development of nanocarrier delivery systems. Self-assembling peptides are emerging in a wide range of biomedical and bioengineering applications and fall into several classes, including peptide amphiphilies, bolaamphiphile peptides, cyclic peptides, and ionic complementary peptides, which can be found naturally or synthesized. The advantage of synthesizing peptides is that their self-assembling properties can be exploited to form desirable structures for various applications. Another, unique property of self-assembling peptides, is stimuli-responsibility in different environments including various pHs, temperatures, ionic strengths, etc. These characteristics make peptides applicable in a wide range of biomaterials in drug discovery. This study reviews the design principles of well-known selfassembling peptides, as well as their physical/chemical properties. In addition, it discusses the therapeutic cancer-targeting peptides and current combinatorial peptide library methods used to identify targeting peptides. Cancer-targeting peptides can target either tumor cell surfaces or tumor vasculature. The RGD peptide is one of the first tumor-targeting peptides that can bind to self-assembling peptides or any other nanocarrier to improve the therapeutic efficiency of targeting drug delivery systems.
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Cite this article as:
Sadatmousavi Parisa, Soltani M., Nazarian Reyhaneh, Jafari Mousa and Chen P., Self-Assembling Peptides: Potential Role in Tumor Targeting, Current Pharmaceutical Biotechnology 2011; 12 (8) . https://dx.doi.org/10.2174/138920111796117409
DOI https://dx.doi.org/10.2174/138920111796117409 |
Print ISSN 1389-2010 |
Publisher Name Bentham Science Publisher |
Online ISSN 1873-4316 |
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