NDLI: Intrinsically disordered amphiphilic peptides as potential targets in drug delivery vehicles.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Vincenzi, Marian Accardo, Antonella Costantini, Susan Scala, Stefania Portella, Luigi Trotta, Annamaria Ronga, Luisa Guillon, Jean Leone, Marilisa Colonna, Giovanni Rossi, Filomena Tesauro, Diego
Description	Country affiliation: Italy Author Affiliation: Vincenzi M ( Department of Pharmacy and CIRPeB University of Naples 'Federico II', Via Mezzocannone 16, I-80134 Naples, Italy. diego.tesauro@unina.it.)
Abstract	Intrinsically disordered proteins/peptides play a crucial role in many physiological and pathological events and may assume a precise conformation upon binding to a specific target. Recently, we have described the conformational and functional properties of two linear ester peptides provided with the following sequences: Y-G-E-C-P-C-K-OAllyl (PepK) and Y-G-E-C-P-C-E-OAllyl (PepE). Both peptides are characterized by the presence of the 'CPC' motif together with a few amino acids able to promote disorder. The CPC sequence is a binding motif for the CXCR4 receptor that represents a well-known target for cancer therapies. In this paper, we report on synthetic amphiphilic peptides that consist of lipophilic derivatives of PepE and PepK bearing two stearic alkyl chains and/or an ethoxylic spacer. These peptide amphiphiles form stable supramolecular aggregates; they present conformational features that are typical of intrinsically disordered molecules as shown by CD spectroscopy. Solution fluorescence and DLS studies have been performed to evaluate Critical Micellar Concentrations and the dimension of supramolecular aggregates. Moreover, preliminary in vitro cell-based assays have been conducted to investigate the molecular recognition processes involving the CXCR4 receptor. In the end, the results obtained have been compared with the previous data generated by the corresponding non-amphiphilic peptides (PepE and PepK).
File Format	HTM / HTML
ISSN	1742206X
Issue Number	11
Volume Number	11
e-ISSN	17422051
Journal	Molecular BioSystems
Language	English
Publisher	Royal Society of Chemistry
Publisher Date	2015-11-01
Publisher Place	Great Britain (UK)
Access Restriction	Subscribed
Subject Keyword	Discipline Molecular Biology Discipline Biochemistry Drug Delivery Systems Intrinsically Disordered Proteins Chemistry Peptides Surface-active Agents Animals Circular Dichroism Cyclic Amp Metabolism Dynamic Light Scattering Fluorescent Dyes Chemical Synthesis Protein Aggregates Receptors, Cxcr4 Spectrometry, Fluorescence Journal Article Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Molecular Biology Biotechnology

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