Abstract
Combinatorial peptide libraries from synthetic or biological sources have been largely used in the last two-decades with the aim of identifying bioactive peptides that specifically bind proteins and modulate their interactions with other protein partners. Differently from biological libraries, synthetic methods allow the development of different kinds of libraries based on two main characteristics: i) the use of building blocks and chemical bonds different from those naturally occurring and ii) the possibility of designing scaffolds with non-linear shapes, as cyclic and branched structures. These two features, alone or in combination, have increased the chemical and structural diversity of peptide libraries expanding the offer of collections for the screenings. Here we describe our and other experiences with branched peptides and the results obtained in the last fifteen years. These clearly indicate how the use of short multimerized peptides can represent a successful approach for different applications ranging from affinity chromatography to the modulation of protein-protein interactions in different biological contexts.
Keywords: Multimeric peptides, combinatorial peptide library, nterleukin-6, immunoglobulin purification, PAM (Protein A Mimetic), Fc receptor, VEGFR-1, Cripto, Hepatitis B virus, Squamous Cell Carcinoma Antigen 1, Neurotensin, TNFα, MAP (Mulptiple Antigen Peptide)
Current Medicinal Chemistry
Title: Branched Peptides for the Modulation of Protein-Protein Interactions: More Arms are Better than One?
Volume: 18 Issue: 16
Author(s): M. Ruvo, A. Sandomenico, L. Tudisco and S. De Falco
Affiliation:
Keywords: Multimeric peptides, combinatorial peptide library, nterleukin-6, immunoglobulin purification, PAM (Protein A Mimetic), Fc receptor, VEGFR-1, Cripto, Hepatitis B virus, Squamous Cell Carcinoma Antigen 1, Neurotensin, TNFα, MAP (Mulptiple Antigen Peptide)
Abstract: Combinatorial peptide libraries from synthetic or biological sources have been largely used in the last two-decades with the aim of identifying bioactive peptides that specifically bind proteins and modulate their interactions with other protein partners. Differently from biological libraries, synthetic methods allow the development of different kinds of libraries based on two main characteristics: i) the use of building blocks and chemical bonds different from those naturally occurring and ii) the possibility of designing scaffolds with non-linear shapes, as cyclic and branched structures. These two features, alone or in combination, have increased the chemical and structural diversity of peptide libraries expanding the offer of collections for the screenings. Here we describe our and other experiences with branched peptides and the results obtained in the last fifteen years. These clearly indicate how the use of short multimerized peptides can represent a successful approach for different applications ranging from affinity chromatography to the modulation of protein-protein interactions in different biological contexts.
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Cite this article as:
Ruvo M., Sandomenico A., Tudisco L. and De Falco S., Branched Peptides for the Modulation of Protein-Protein Interactions: More Arms are Better than One?, Current Medicinal Chemistry 2011; 18 (16) . https://dx.doi.org/10.2174/092986711795843191
DOI https://dx.doi.org/10.2174/092986711795843191 |
Print ISSN 0929-8673 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-533X |
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