Luciano Galantini

Prof. Luciano Galantini

Sapienza Università di Roma, Chemistry Department
orcid

Research Focus & Metrics

Academic Career Length

36Years (1991-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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MGMaria Chiara di Gregorio
Maria Chiara di Gregorio
Jacopo CautelaJacopo Cautela
Jacopo Cautela
Luciano GalantiniLuciano Galantini
Luciano Galantini
Bile acids (BAs) are facial amphiphiles synthesized in the body of all vertebrates. They undergo the enterohepatic circulation: they are produced in the liver, stored in the gallbladder, released in the intestine, taken into the bloodstream and lastly re-absorbed in the liver. During this pathway, BAs are modified in their molecular structure by the action of enzymes and bacteria. Such transformations allow them to acquire the chemical–physical properties needed for fulling several activities including metabolic regulation, antimicrobial functions and solubilization of lipids in digestion. The versatility of BAs in the physiological functions has inspired their use in many bio-applications, making them important tools for active molecule delivery, metabolic disease treatments and emulsification processes in food and drug industries. Moreover, moving over the borders of the biological field, BAs have been largely investigated as building blocks for the construction of supramolecular aggregates having peculiar structural, mechanical, chemical and optical properties. The review starts with a biological analysis of the BAs functions before progressively switching to a general overview of BAs in pharmacology and medicine applications. Lastly the focus moves to the BAs use in material science.

20 September 2018 in Langmuir
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MGMaria Chiara di Gregorio
Maria Chiara di Gregorio
LTLeana Travaglini
Leana Travaglini
AGAlessandra Del Giudice
Alessandra Del Giudice
Jacopo CautelaJacopo Cautela
Jacopo Cautela
NPNicolae Viorel Pavel
Nicolae Viorel Pavel
Luciano GalantiniLuciano Galantini
Luciano Galantini

7 April 2006 in Journal of the American Chemical Society
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Journal Article
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VTVictor Hugo Soto Tellini
Victor Hugo Soto Tellini
ARAida Jover Ramos
Aida Jover Ramos
JGJorge Carrazana García
Jorge Carrazana García
Luciano GalantiniLuciano Galantini
Luciano Galantini
FMFrancisco Meijide
Francisco Meijide
JTJosé Vázquez Tato
José Vázquez Tato

1 June 2015 in Current Opinion in Colloid & Interface Science
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Luciano GalantiniLuciano Galantini
Luciano Galantini
MGM. Chiara di Gregorio
M. Chiara di Gregorio
MGMarta Gubitosi
Marta Gubitosi
LTLeana Travaglini
Leana Travaglini
JTJosé Vázquez Tato
José Vázquez Tato
NPNicolae V. Pavel
Nicolae V. Pavel

18 September 2008 in Physical Chemistry Chemical Physics
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MLMaria Leggio
Maria Leggio
Luciano GalantiniLuciano Galantini
Luciano Galantini
NPNicolae Viorel Pavel
Nicolae Viorel Pavel
A structural comparison between the Normal and the Expanded isomers of the human serum albumin has been carried out by using small angle X-ray scattering (SAXS) and light scattering (LS) techniques. Geometrical bodies, recovered structures (GA_STRUCT code) and rigid body modeling (CRYSOL and BUNCH software) were used to obtain low-resolution 3D structures from one-dimensional scattering patterns. These restored shapes were also exploited to perform a correlation between SAXS and LS data. By attempting a detailed description of globular and unfolded protein structures in solution, we tried to propose a suitable approach to follow the path of folding/unfolding processes and to isolate and characterize possible partially folded intermediate states.

28 September 2005 in Langmuir
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Cecilia BombelliCecilia Bombelli
Cecilia Bombelli
SBStefano Borocci
Stefano Borocci
MDMarco Diociaiuti
Marco Diociaiuti
Francesca FaggioliFrancesca Faggioli
Francesca Faggioli
Luciano GalantiniLuciano Galantini
Luciano Galantini
MSMaria Grazia Sacco
Maria Grazia Sacco