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      Peptide-Based Drug-Delivery Systems in Biotechnological Applications: Recent Advances and Perspectives

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          Abstract

          Peptides of natural and synthetic sources are compounds operating in a wide range of biological interactions. They play a key role in biotechnological applications as both therapeutic and diagnostic tools. They are easily synthesized thanks to solid-phase peptide devices where the amino acid sequence can be exactly selected at molecular levels, by tuning the basic units. Recently, peptides achieved resounding success in drug delivery and in nanomedicine smart applications. These applications are the most significant challenge of recent decades: they can selectively deliver drugs to only pathological tissues whilst saving the other districts of the body. This specific feature allows a reduction in the drug side effects and increases the drug efficacy. In this context, peptide-based aggregates present many advantages, including biocompatibility, high drug loading capacities, chemical diversity, specific targeting, and stimuli responsive drug delivery. A dual behavior is observed: on the one hand they can fulfill a structural and bioactive role. In this review, we focus on the design and the characterization of drug delivery systems using peptide-based carriers; moreover, we will also highlight the peptide ability to self-assemble and to actively address nanosystems toward specific targets.

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          Most cited references141

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          RGD-based strategies to target alpha(v) beta(3) integrin in cancer therapy and diagnosis.

          The integrin α(v)β(3) plays an important role in angiogenesis. It is expressed on tumoral endothelial cells as well as on some tumor cells. RGD peptides are well-known to bind preferentially to the α(v)β(3) integrin. In this context, targeting tumor cells or tumor vasculature by RGD-based strategies is a promising approach for delivering anticancer drugs or contrast agents for cancer therapy and diagnosis. RGD-based strategies include antagonist drugs (peptidic or peptidomimetic) of the RGD sequence, RGD-conjugates, and the grafting of the RGD peptide or peptidomimetic, as targeting ligand, at the surface of nanocarriers. Although all strategies are overviewed, this review aims to particularly highlight the position of RGD-based nanoparticles in cancer therapy and imaging. This review is divided into three parts: the first one describes the context of angiogenesis, the role of the integrin α(v)β(3), and the binding of the RGD peptide to this integrin; the second one focuses on RGD-based strategies in cancer therapy; while the third one focuses on RGD-based strategies in cancer diagnosis.
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            Nanostructured Hydrogels for Three-Dimensional Cell Culture Through Self-Assembly of Fluorenylmethoxycarbonyl–Dipeptides

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              Self-assembly and application of diphenylalanine-based nanostructures.

              Micro- and nanostructures fabricated from biological building blocks have attracted tremendous attention owing to their potential for application in biology and in nanotechnology. Many biomolecules, including peptides and proteins, can interact and self-assemble into highly ordered supramolecular architectures with functionality. By imitating the processes where biological peptides or proteins are assembled in nature, one can delicately design and synthesize various peptide building blocks composed of several to dozens of amino acids for the creation of biomimetic or bioinspired nanostructured materials. This tutorial review aims to introduce a new kind of peptide building block, the diphenylalanine motif, extracted with inspiration of a pathogenic process towards molecular self-assembly. We highlight recent and current advances in fabrication and application of diphenylalanine-based peptide nanomaterials. We also highlight the preparation of such peptide-based nanostructures as nanotubes, spherical vesicles, nanofibrils, nanowires and hybrids through self-assembly, the improvement of their properties and the extension of their applications.
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                Author and article information

                Contributors
                Role: Academic Editor
                Role: Academic Editor
                Journal
                Molecules
                Molecules
                molecules
                Molecules
                MDPI
                1420-3049
                19 January 2019
                January 2019
                : 24
                : 2
                : 351
                Affiliations
                [1 ]Department of Pharmacy and CIRPeB, Università Federico II, 80134 Naples, Italy; diego.tesauro@ 123456unina.it (D.T.); antonella.accardo@ 123456unina.it (A.A.); carlo.diaferia@ 123456unina.it (C.D.); vittoria.milano@ 123456unina.it (V.M.)
                [2 ]ARNA, INSERM U1212/UMR CNRS 5320, UFR des Sciences Pharmaceutiques, Université de Bordeaux, F-33000 Bordeaux, France; jean.guillon@ 123456u-bordeaux.fr
                [3 ]Institute of Analytical Sciences, IPREM, UMR 5254, CNRS-University of Pau, 64000 Pau, France; luisa.ronga@ 123456univ-pau.fr
                Author notes
                [* ]Correspondence: filomena.rossi@ 123456unina.it ; Tel.: +39-081-253-6682
                Author information
                https://orcid.org/0000-0002-9273-0136
                https://orcid.org/0000-0001-8577-3894
                Article
                molecules-24-00351
                10.3390/molecules24020351
                6359574
                30669445
                18fe3595-6db0-4582-97b5-17d134e672be
                © 2019 by the authors.

                Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

                History
                : 17 December 2018
                : 18 January 2019
                Categories
                Review

                peptide,peptide backbone structures,drug delivery,peptide self-assembling carriers,active targeting receptors,diphenylalanine,binding peptides

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