Leila Birolo

University of Naples Federico II

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Gennaro Marino

University of Naples Federico II

Piero Pucci

University of Naples Federico II

Giovanni Sannia

Federico II University Hospital

Roberto Vinciguerra

University of Naples Federico II

Ilaria Bonaduce

University of Pisa

Georgia Ntasi

University of Naples Federico II

G. Leo

Policlinico di Modena

Vincenza Faraco

University of Naples Federico II

Alessandro Vergara

University of Naples Federico II

Angela Amoresano

University of Naples Federico II

Cooperative Institutions

University of Naples Federico II

153

Federico II University Hospital

Istituto Nazionale di Fisica Nucleare, Sezione di Napoli

National Research Council

Naples Anesthesia & Physician Associates

Ceinge Biotecnologie Avanzate (Italy)

University of Pisa

National Academies of Sciences, Engineering, and Medicine

University of Florence

Istituto Nazionale Biostrutture e Biosistemi

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Exploitation of proteomics strategies in protein structure-function studies

Pure and Applied Chemistry (2003)

Gennaro Marino Piero Pucci Leila Birolo Margherita Ruoppolo

Abstract Mass spectrometry plays a central role in structural proteomics, particularly in highly intensive structural genomics projects. This review paper reports some examples taken from recent work from the authors' laboratory and is aimed at showing that modern proteomics strategies are instrumental in the integration of structural genomic projects in fields such as: (i) protein–protein interactions, (ii) protein-DNA interactions, (iii) protein–ligand interactions, and (iv) protein-folding intermediates.

Structural genomics

Folding (DSP implementation)

Protein chemistry

10.1351/pac200375020309

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Citations (5)

Folding factors from a cold adapted microorganism

Comparative Biochemistry and Physiology Part A Molecular & Integrative Physiology (2000)

Leila Birolo Gennaro Marino

Folding (DSP implementation)

10.1016/s1095-6433(00)80198-1

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Citations (0)

1H and 15N Chemical Shift Assignments for Titin Z-repeat 7 in the Complex with Alpha-actinin C-terminal EF-hands

Journal of Back and Musculoskeletal Rehabilitation (2000)

Roger Atkinson Catherine Joseph Fabrizio Dal Piaz Leila Birolo Günter Stier

Alpha (finance)

10.13018/bmr4454

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Hexafluoroisopropanol and Acid Destabilized Forms of Apomyoglobin Exhibit Structural Differences

Biochemistry (2002)

Ivana Sirangelo Fabrizio Dal Piaz Clorinda Malmo Mariateresa Casillo Leila Birolo

The conformational properties of partially folded states of apomyoglobin have been investigated using an integrated approach based on fluorescence spectroscopy and hydrogen/deuterium exchange followed by mass spectrometry. The examined states were those obtained: (i) by adding 4% v/v hexafluoroisopropanol to native myoglobin, HFIP-MGN; (ii) by adding 4% v/v hexafluoroisopropanol to acid unfolded myoglobin, HFIP-MGU; (iii) at pH 3.8, I-1 state; and (iv) at pH 2.0−0.2 M NaCl, A state. Proteolytic digestion of the hydrogen/deuterium exchanged proteins showed that, in I-1 state, the helices C, D, E, and F incorporate more deuterium, whereas in HFIP-MGN the exchange rate is similar for all protein regions. These results suggest that I-1 contains the ABGH domain in a native-like organization, whereas HFIP-MGN loses a large number of tertiary interactions, thus acquiring a more flexible structure. The fluorescence data are consistent with the above picture. In fact, the tryptophan/ANS energy transfer is much less efficient for the ANS−HFIP-MGN complex than for the other complexes, thus suggesting that the distances between the fluorophores might be increased. Moreover, fluorescence polarization measurements indicated that the rotational motion of HFIP-MGN occurs on a longer time scale than the other partially folded states, thus suggesting that the volume of this state could be larger. The overall results indicate that addition of hexafluoroisopropanol to native myoglobin results in the formation of a true molten globule where tertiary interactions are reduced, while the secondary structure and the globular compactness are conserved.

Hydrogen–deuterium exchange

Molten globule

Protein tertiary structure

10.1021/bi020447f

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Citations (26)

Conformational Analysis of Rat Seminal Vesicle Secretory Protein 4, an Intrinsically Disordered Protein Having Interesting Pharmacological Properties

International Journal of Chemistry (2015)

Susan Costantini Vasu Gautam Salvatore Di Maria Leila Birolo Sara Longobardi

Rat seminal vesicle protein 4 (RSV4) is a member of the seminal vesicle protein family present in rats, 90 residues long. When secreted, it is involved in many functions related to the reproduction ranging from semen coagulation to sperm capacitation, but its fragments have also shown in vitro pharmacological properties such as anti-inflammatory and pro-coagulant activity, important in the cancer development. However, no three-dimensional model of this protein is yet available probably because of the presence of intrinsic disorder in the structure. In this article we report structural studies in solution of RSV4 by SEC (size exclusion chromatography) and CD (circular dichroism). In solution the monomer is highly flexible and poorly organized with the presence of highly fluctuating helical segments and, as also suggested by SEC, is classifiable as NU-PMG (natively unfolded pre-molten globule). The lack of a cooperative sigmoidal structural transition induced by thermal and GdmCl perturbation in monomer supports the poor structural organization expected for a NU-PMG conformational model. The structure of RSV4 monomer was modeled computationally and subjected to molecular dynamics simulations to study its conformational changes and energetic stability.

Capacitation

10.5539/ijc.v7n2p133

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Functional and Structural Analysis of cis-Proline Mutants of Escherichia coli Aspartate Aminotransferase^,

Biochemistry (1998)

Leila Birolo V.N. Malashkevich Guido Capitani F. De Luca Alma Moretta

To elucidate the role of the two conserved cis-proline residues of aspartate aminotransferase (AspAT), one double and two single mutants of the enzyme from Escherichia coli (EcAspAT) were prepared: P138A, P195A and P138A/P195A in which the two prolines were replaced by alanine. The crystal structures of P195A and P138A/P195A have been determined at 2.3−2.1 Å resolution. The wild-type geometry, including the cis conformation of the 194−195 peptide bond is retained upon substitution of proline 195 by alanine, whereas the trans conformation is adopted at the 137−138 peptide bond. Quite surprisingly, the replacement of each of the two prolines by alanine does not significantly affect either the activity or the stability of the protein. All the three mutants follow the same pathway as the wild type for unfolding equilibrium induced by guanidine hydrochloride [Herold, M., and Kirschner, K. (1990) Biochemistry 29, 1907−1913]. The kinetics of renaturation of P195A, where the alanine retains the wild-type cis conformation, is faster than wild type, whereas renaturation of P138A, which adopts the trans conformation, is slower. We conclude that cis-prolines seem to have been retained throughout the evolution of aspartate aminotransferase to possibly play a subtle role in directing the traffic of intermediates toward the unique structure of the native state, rather than to respond to the needs for a specific catalytic or functional role.

10.1021/bi981467d

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Citations (23)

Proteomics and spectroscopic analyses for the molecular characterization of collagen-based animal glues

Georgia Ntasi Brunella Cipolletta Carmen Aprea Laura Dello Ioio Celia Duce

Animal glues are widely used in restoration, as adhesives, binders and consolidants for organic and inorganic materials.Their variable performances are intrinsically linked to the adhesive characteristics of collagen, which determines the chemical, physical and mechanical properties of the glue.In this work, a multi-analytical approach based on proteomics and spectroscopic analyses is used to characterize a set of animal glues from different sources provided by restoration workshops.Shotgun proteomic analysis provided animal origin, even when blended, and allowed to distinguish between hide and bone glue on the basis of the presence of collagen type III.Proteomics and analytical pyrolysis coupled to GC-MS have been used to analyse chemical modifications in collagen, demonstrating their variability among different glues and showing that, on average, bone glues are less deamidated than hide glues, but more fragmented, and mixed-collagen glues are overall less deamidated than pure glues.Spectroscopic analyses have also been exploited to gain insights in structural changes occurring upon glue preparation from natural materials.

Characterization

10.21014/10.21014/tc4-arc-2023.132

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Proteomic Characterization of Collagen-Based Animal Glues for Restoration

Journal of Proteome Research (2022)

Georgia Ntasi Sara Sbriglia Rossana Pitocchi Roberto Vinciguerra Chiara Melchiorre

Animal glues are widely used in restoration as adhesives, binders, and consolidants for organic and inorganic materials. Their variable performances are intrinsically linked to the adhesive properties of collagen, which determine the chemical, physical, and mechanical properties of the glue. We have molecularly characterized the protein components of a range of homemade and commercial glues using mass spectrometry techniques. A shotgun proteomic analysis provided animal origin, even when blended, and allowed us to distinguish between hide and bone glue on the basis of the presence of collagen type III, which is abundant in connective skin/leather tissues and poorly synthetized in bones. Furthermore, chemical modifications, a consequence of the preparation protocols from the original animal tissue, were thoroughly evaluated. Deamidation, methionine oxidation, and backbone cleavage have been analyzed as major collagen modifications, demonstrating their variability among different glues and showing that, on average, bone glues are less deamidated than hide glues, but more fragmented, and mixed-collagen glues are overall less deamidated than pure glues. We believe that these data may be of general analytical interest in the characterization of collagen-based materials and may help restorers in the selection of the most appropriate materials to be used in conservation treatments.

Deamidation

Characterization

10.1021/acs.jproteome.2c00232

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Citations (17)

A simple and reliable methodology to detect egg white in art samples

Journal of Biosciences (2013)

Michela Gambino Francesca Cappitelli Cristina Cattò Aristodemo Carpen Pamela Principi

Matrix (chemical analysis)

10.1007/s12038-013-9321-z

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Citations (30)

Minimally Invasive and Portable Method for the Identification of Proteins in Ancient Paintings

Analytical Chemistry (2018)

Paola Cicatiello Georgia Ntasi Manuela Rossi Gennaro Marino Paola Giardina

A novel method for the analysis of proteinaceous materials present on painted surfaces was developed by taking advantage of the adhesive ability of some fungal proteins which can form a stable and homogeneous layer on flexible transparency sheets able to capture trypsin in a fully active form. We demonstrated that the bioactive sheets were able to efficiently digest proteins, present as such, on surfaces of painted tests and historical samples, releasing peptides that can allow an easy and confident identification of the proteinaceous binders by standard bottom-up proteomic approach. By this method there is no need: (i) to transport the artifacts and (ii) to remove, even at micro level, a sample from the object. The ingenuity of the method lies in the easily accommodated sampling coupled with a minimal invasiveness.

Ingenuity

Sample Preparation

10.1021/acs.analchem.8b01718

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Citations (34)