Understanding the Structural Requirements of Peptide-Protein Interaction and Applications for Peptidomimetic Development.

Autor:	Macias ALD; Biochemistry Department, Institute of Chemistry, University of Sao Paulo, Sao Paulo, Brazil., Alecrim LC; Biochemistry Department, Institute of Chemistry, University of Sao Paulo, Sao Paulo, Brazil., Almeida FCL; Institute of Medical Biochemistry, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil., Giordano RJ; Biochemistry Department, Institute of Chemistry, University of Sao Paulo, Sao Paulo, Brazil. giordano@iq.usp.br.
Jazyk:	angličtina
Zdroj:	Methods in molecular biology (Clifton, N.J.) [Methods Mol Biol] 2024; Vol. 2793, pp. 65-82.
DOI:	10.1007/978-1-0716-3798-2_5
Abstrakt:	Protein-protein interaction is at the heart of most biological processes, and small peptides that bind to protein binding sites are resourceful tools to explore and understand the structural requirements for these interactions. In that sense, phage display is a well-suited technology to study protein-protein interactions, as it allows for unbiased screening of billions of peptides in search for those that interact with a protein binding domain. Here, we will illustrate how two distinct but complementary approaches, phage display and nuclear magnetic resonance (NMR), can be utilized to unveil structural details of peptide-protein interaction. Finally, knowledge derived from phage mutagenesis and NMR studies can be streamlined for quick peptidomimetic design and synthesis using the retroinversion approach to validate using in vitro and in vivo assays the therapeutic potential of peptides identified by phage display. (© 2024. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.)
Databáze:	MEDLINE
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