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Branched Peptides for the Modulation of Protein-Protein Interactions: More Arms are Better than One?

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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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Keywords: Cripto; Fc receptor; Hepatitis B virus; MAP (Mulptiple Antigen Peptide); Multimeric peptides; Neurotensin; PAM (Protein A Mimetic); Squamous Cell Carcinoma Antigen 1; TNFα; VEGFR-1; combinatorial peptide library; immunoglobulin purification; nterleukin-6

Document Type: Research Article

Publication date: 2011-06-01

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  • Current Medicinal Chemistry covers all the latest and outstanding developments in medicinal chemistry and rational drug design. Each issue contains a series of timely in-depth reviews written by leaders in the field covering a range of the current topics in medicinal chemistry. Current Medicinal Chemistry is an essential journal for every medicinal chemist who wishes to be kept informed and up-to-date with the latest and most important developments.
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