Owing to the large panel of biological functions of peptides and their high specificity and potency, the development of peptide-based therapeutic and diagnostic tools has received increased interest. Peptide amphiphiles (PAs) are an emerging class of molecules in which a bioactive peptide is covalently conjugate to a hydrophobic moiety. Due to the coexistence in the molecule of a hydrophilic peptide sequence and a hydrophobic group, PAs are able to selfassemble spontaneously into a variety of nanostructures, such as monolayers, bilayers, and vesicles. In this work we have synthesized predicted by MEDOR disordered peptide sequences3 functionalized by alkyl chains, and connected by ethoxylic-based linker. The structural properties in solution of these new PAs were investigated using CD, NMR and DLS. The presence of the alkyl chains induces not only the self-assembly of these new PAs into supramolecular aggregates but also a gain of structure within the disordered peptide. The design of supramolecular systems, generated by joining a disordered peptide and a lipophilic moiety, could drive the disordered peptide to fold into a stable structure. This structural modification could be a promising route to develop a new class of bio-molecules for processes in which a specific conformational rearrangement is required.

CD and NMR Conformational Preferences of Intrinsically Disordered Amphiphilic Peptides: A New Class of Potential Targets in Drug Discovery / Tesauro, Diego; Vincenzi, Marian; Flavia A., Mercurio; Accardo, Antonella; Luisa, Ronga; Marilisa, Leone; Rossi, Filomena. - (2014), pp. 60-60. (Intervento presentato al convegno Disordered Motifs and Domains in Cell Control tenutosi a Dublino nel 11-15 Ottobre 2014).

CD and NMR Conformational Preferences of Intrinsically Disordered Amphiphilic Peptides: A New Class of Potential Targets in Drug Discovery

TESAURO, DIEGO
;
VINCENZI, MARIAN
Membro del Collaboration Group
;
ACCARDO, ANTONELLA
Membro del Collaboration Group
;
ROSSI, FILOMENA
2014

Abstract

Owing to the large panel of biological functions of peptides and their high specificity and potency, the development of peptide-based therapeutic and diagnostic tools has received increased interest. Peptide amphiphiles (PAs) are an emerging class of molecules in which a bioactive peptide is covalently conjugate to a hydrophobic moiety. Due to the coexistence in the molecule of a hydrophilic peptide sequence and a hydrophobic group, PAs are able to selfassemble spontaneously into a variety of nanostructures, such as monolayers, bilayers, and vesicles. In this work we have synthesized predicted by MEDOR disordered peptide sequences3 functionalized by alkyl chains, and connected by ethoxylic-based linker. The structural properties in solution of these new PAs were investigated using CD, NMR and DLS. The presence of the alkyl chains induces not only the self-assembly of these new PAs into supramolecular aggregates but also a gain of structure within the disordered peptide. The design of supramolecular systems, generated by joining a disordered peptide and a lipophilic moiety, could drive the disordered peptide to fold into a stable structure. This structural modification could be a promising route to develop a new class of bio-molecules for processes in which a specific conformational rearrangement is required.
2014
CD and NMR Conformational Preferences of Intrinsically Disordered Amphiphilic Peptides: A New Class of Potential Targets in Drug Discovery / Tesauro, Diego; Vincenzi, Marian; Flavia A., Mercurio; Accardo, Antonella; Luisa, Ronga; Marilisa, Leone; Rossi, Filomena. - (2014), pp. 60-60. (Intervento presentato al convegno Disordered Motifs and Domains in Cell Control tenutosi a Dublino nel 11-15 Ottobre 2014).
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11588/598802
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