Antonia De Capua

University of Naples Federico II

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Ettore Benedetti

University of Naples Federico II

Daniela Marasco

University of Naples Federico II

Menotti Ruvo

Institute of Biostructure and Bioimaging

Carlo Pedone

Institute of Biostructure and Bioimaging

Paolo A. Netti

University of Naples Federico II

Michele Saviano

Institute of Crystallography

Filomena Rossi

University of Naples Federico II

Teodorico Tancredi

Istituto di Chimica Biomolecolare

Gennaro Piccialli

University of Naples Federico II

Gabriella Saviano

University of Molise

Cooperative Institutions

University of Naples Federico II

Institute of Biostructure and Bioimaging

Centro Interuniversitario di Ricerca sui Peptidi Bioattivi

National Research Council

Federico II University Hospital

National Academies of Sciences, Engineering, and Medicine

Istituto Nazionale di Fisica Nucleare, Sezione di Napoli

Naples Anesthesia & Physician Associates

Institute for Experimental Endocrinology and Oncology

Istituto Nazionale Tumori IRCCS "Fondazione G. Pascale"

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A New Ligand for Immunoglobulin G Subdomains by Screening of a Synthetic Peptide Library

ChemBioChem (2005)

Antonio Verdoliva Daniela Marasco Antonia De Capua Angela Saporito Piero Bellofiore

Abstract By screening a synthetic peptide library of general formula (NH 2 ‐Cys1‐X2‐X3‐X4) 2 ‐Lys‐Gly‐OH, a disulfide‐bridged cyclic peptide, where X2‐X3‐X4 is the tripeptide Phe‐His‐His, has been selected as a ligand for immunoglobulin G (IgG). The peptide, after a preliminary chromatographic characterization, has proved useful as a new affinity ligand for the purification of polyclonal as well as monoclonal antibodies from biological fluids, with recovery yields of up to 90 % (90 % purity). The ligand is able to bind antibody fragments containing both Fab and Fc from different antibody isotypes, a fact suggesting the presence of at least two different antibody‐binding sites. While the recognition site on Fab is unknown, comparative binding studies with Fc, in association with the striking similarities of the peptide (named Fc‐receptor mimetic, FcRM) with a region of the human FcγRIII receptor, strongly indicate that the peptide could recognize a short amino acid stretch of the lower hinge region, which has a key role in autoimmune disease triggering. The unique properties make the ligand attractive for both the purification of antibody fragments and as a lead for the generation of Fc‐receptor antagonists.

Tripeptide

Polyclonal antibodies

10.1002/cbic.200400368

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Citations (46)

The human prion protein α2 helix: A thermodynamic study of its conformational preferences

Proteins Structure Function and Bioinformatics (2005)

Barbara Tizzano Pasquale Palladino Antonia De Capua Daniela Marasco Filomena Rossi

Abstract We have synthesized both free and terminally‐blocked peptide corresponding to the second helical region of the globular domain of normal human prion protein, which has recently gained the attention of structural biologists because of a possible role in the nucleation process and fibrillization of prion protein. The profile of the circular dichroism spectrum of the free peptide was that typical of α‐helix, but was converted to that of β‐structure in about 16 h. Instead, below 2.1 × 10 −5 M, the spectrum of the blocked peptide exhibited a single band centered at 200 nm, unequivocally associated to random conformations, which did not evolve even after 24 h. Conformational preferences of this last peptide have been investigated as a function of temperature, using trifluoroethanol or low‐concentration sodium dodecyl sulfate as α‐ or β‐structure inducers, respectively. Extrapolation of free energy data to zero concentration of structuring agent highlighted that the peptide prefers α‐helical to β‐type organization, in spite of results from prediction algorithms. However, the free energy difference between the two forms, as obtained by a thermodynamic cycle, is subtle (roughly 5–8 kJ mol −1 at any temperature from 280 K to 350 K), suggesting conformational ambivalence. This result supports the view that, in the prion protein, the structural behavior of the peptide is governed by the cellular microenvironment. Proteins 2005. © 2005 Wiley‐Liss, Inc.

Helix (gastropod)

Globular protein

Sodium dodecyl sulfate

10.1002/prot.20395

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Citations (40)

Engineering of Covalently Immobilized Gradients of RGD Peptides on Hydrogel Scaffolds: Effect on Cell Behaviour

Macromolecular Symposia (2008)

Daniela Guarnieri Assunta Borzacchiello Antonia De Capua Menotti Ruvo Paolo A. Netti

Abstract Summary: The aim of this study has been to design a system for the preparation of Polyethylene‐glycol (PEG) based hydrogels with a controlled spatial distribution of covalently immobilised RGD adhesion signals in order to control and guide cell response for tissue engineering application. Gradients of immobilised RGD peptides were characterized by confocal microscopy analysis. Moreover, the effect of RGD spatial distribution on cell behaviour was evaluated by using mouse embryo fibroblasts NIH3T3. In particular, we observed cell adhesion and migration of fibroblasts seeded on RGD gradient compared to cells on control hydrogels having an uniform distribution of RGD. Our data suggest that a linear gradient of covalently immobilised adhesion signals affects cell behaviour. In particular, cells feel RGD gradient and oriented themselves and move along gradient direction.

10.1002/masy.200850607

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Citations (17)

Surface bio-functionalization for mesenchymal stem cells-trapping onto prosthetic surfaces

Paolo Giannoni Maria Iannone Antonia De Capua Rodolfo Quarto Paolo A. Netti

Surface Modification

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A New Ligand for Immunoglobulin G Subdomains by Screening of a Synthetic Peptide Library

ChemBioChem (2005)

Antonio Verdoliva Daniela Marasco Antonia De Capua Angela Saporito Piero Bellofiore

In issue 7, Figure 61 on page 1251 was inadequately printed and should have appeared as shown below. The printers apologise for this error.

10.1002/cbic.200590026

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Citations (1)

Protein–Protein Interactions: A Simple Strategy to Identify Binding Sites and Peptide Antagonists

Chemical Biology & Drug Design (2009)

Annamaria Sandomenico Simona Maria Monti Marco Sabatella Antonia De Capua Laura Tornatore

Secondary structure motifs and small protein domains can act as building blocks that are isolated and investigated to gain insights into protein global structure but can also modulate interactions with external partners. Most progress has been made in this field using synthetic peptides. Fragmentation of folded proteins by proteolytic enzymes that act preferentially on exposed and less structured sites can help to isolate shorter polypeptides with preserved secondary and tertiary structures that mimic the original protein architecture. Such molecules can be used as probes for structural studies and as tools for in vitro assays to select active fragments useful as agonists or antagonists of the original protein or as scaffolds for the design of more potent and selective ligands. This simple but effective proteolytic methodology has been successfully applied to determine antagonists of protein–protein interactions, allowing the identification of inhibitors with high efficacy and specificity. Here, we present several studies including the complex between phosphoprotein enriched in diabetes/phosphoprotein enriched in astrocytes and phospholipase 1, believed to play a relevant role in the insulin resistance mechanism in phosphoprotein enriched in diabetes/phosphoprotein enriched in astrocytes‐overexpressing tissues, the self‐association of BCL10 caspase recruitment domain that mediates a protein oligomerization process responsible for NF‐κB activation and the self‐association of growth arrest and DNA damage‐inducible factor 45β, a major player of the endogenous NF‐κB‐mediated resistance to apoptosis.

Phosphoprotein

10.1111/j.1747-0285.2009.00805.x

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Citations (14)

Interaction between ghrelin and the ghrelin receptor (GHS-R1a), a NMR study using living cells

Bioorganic & Medicinal Chemistry (2010)

Manuel Martín‐Pastor Antonia De Capua C. J. Álvarez Dolores Díaz Jesús Jiménez‐Barbero

Conformational isomerism

Chemical shift

10.1016/j.bmc.2010.01.004

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Citations (15)

A New Strategy for the Solid-Phase Synthesis of Glycoconjugate Biomolecules

Synlett (2001)

Giovanni Di Fabio Antonia De Capua Lorenzo De Napoli Daniela Montesarchio Gennaro Piccialli

A simple and efficient bidirectional solid-phase synthesis, based on the use of a Tentagel solid support, functionalized with a suitably protected 2-amino sugar residue, is proposed for the preparation of a variety of glycoconjugates, including glycopeptides and nucleo-glycopeptides.

Glycoconjugate

Solid-Phase Synthesis

Biomolecule

Residue (chemistry)

10.1055/s-2001-11391

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Citations (8)

Generation and functional characterization of a BCL10-inhibitory peptide that represses NF-κB activation

Biochemical Journal (2009)

Daniela Marasco Romania Stilo Annamaria Sandomenico Simona Maria Monti Barbara Tizzano

The molecular complex containing BCL10 and CARMA [CARD (caspase recruitment domain)-containing MAGUK (membrane-associated guanylate kinase)] proteins has recently been identified as a key component in the signal transduction pathways that regulate activation of the transcription factor NF-κB (nuclear factor κB) in lymphoid and non-lymphoid cells. Assembly of complexes containing BCL10 and CARMA proteins relies on homophilic interactions established between the CARDs of these proteins. In order to identify BCL10-inhibitory peptides, we have established a method of assaying peptides derived from the CARD of BCL10 in binding competition assays of CARD–CARD self-association. By this procedure, a short peptide corresponding to amino acid residues 91–98 of BCL10 has been selected as an effective inhibitor of protein self-association. When tested in cell assays for its capacity to block NF-κB activation, this peptide represses activation of NF-κB mediated by BCL10, CARMA3 and PMA/ionomycin stimulation. Collectively, these results indicate that residues 91–98 of BCL10 are involved in BCL10 self-association and also participate in the interaction with external partners. We also show that blocking of the CARD of BCL10 may potentially be used for the treatment of pathological conditions associated with inappropriate NF-κB activation.

BCL10

Ionomycin

10.1042/bj20090055

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Citations (11)

Gene-activated and cell-migration guiding PEG matrices based on three dimensional patterning of RGD peptides and DNA complexes

Acta Biomaterialia (2012)

Silvia Orsi Daniela Guarnieri Antonia De Capua Paolo A. Netti

Matrix (chemical analysis)

10.1016/j.actbio.2012.05.010

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Citations (8)