The human hepcidin-25 hormone has a key role in iron regulation in blood. The clinical relevance of this hepatic ~2.8. kDa cysteine-rich peptide is rapidly increasing, since altered levels can be associated with inflammatory events and iron dysfunctions, such as hereditary hemochromatosis and iron overload. Moreover, hepcidin has also attracted the anti-doping field for its possible role as indirect marker of erythropoietin blood doping. Methods currently reported are based on immunoassays (ELISA and RIA), or various types of mass spectroscopy (MS)-based protocols, semi-quantitative or quantitative. Despite the great effort in optimizing robust and simple assays measuring hepcidin in real matrices, at present this challenge remains still an open issue. To explore the possibility to face hepcidin detection through the development of affinity-based biosensors, we set up a comparative study by surface plasmon resonance (SPR) technology. An immuno-based, on anti-hepcidin-25 IgG, and a biomimetic-based, on a synthetic peptide corresponding to the hepcidin-binding site on ferroportin (HBD), biosensors were developed. Here we report behaviors and analytical performances of the two systems, discussing limits and potentialities. © 2012 Elsevier B.V.

SPR detection of human Hepcidin-25: a critical approach by immuno- and biomimetic-based biosensing / S. Scarano; A. Vestri; M. L. Ermini; M. Minunni. - In: BIOSENSORS & BIOELECTRONICS. - ISSN 0956-5663. - ELETTRONICO. - 40:(2013), pp. 135-140. [10.1016/j.bios.2012.06.060]

SPR detection of human Hepcidin-25: a critical approach by immuno- and biomimetic-based biosensing

SCARANO, SIMONA;ERMINI, MARIA LAURA;MINUNNI, MARIA
2013

Abstract

The human hepcidin-25 hormone has a key role in iron regulation in blood. The clinical relevance of this hepatic ~2.8. kDa cysteine-rich peptide is rapidly increasing, since altered levels can be associated with inflammatory events and iron dysfunctions, such as hereditary hemochromatosis and iron overload. Moreover, hepcidin has also attracted the anti-doping field for its possible role as indirect marker of erythropoietin blood doping. Methods currently reported are based on immunoassays (ELISA and RIA), or various types of mass spectroscopy (MS)-based protocols, semi-quantitative or quantitative. Despite the great effort in optimizing robust and simple assays measuring hepcidin in real matrices, at present this challenge remains still an open issue. To explore the possibility to face hepcidin detection through the development of affinity-based biosensors, we set up a comparative study by surface plasmon resonance (SPR) technology. An immuno-based, on anti-hepcidin-25 IgG, and a biomimetic-based, on a synthetic peptide corresponding to the hepcidin-binding site on ferroportin (HBD), biosensors were developed. Here we report behaviors and analytical performances of the two systems, discussing limits and potentialities. © 2012 Elsevier B.V.
2013
40
135
140
S. Scarano; A. Vestri; M. L. Ermini; M. Minunni
File in questo prodotto:
File Dimensione Formato  
Abstract Hepcidin.docx

accesso aperto

Tipologia: Altro
Licenza: Open Access
Dimensione 59.83 kB
Formato Microsoft Word XML
59.83 kB Microsoft Word XML
Scarano Hepcidin .pdf

Accesso chiuso

Tipologia: Versione finale referata (Postprint, Accepted manuscript)
Licenza: Tutti i diritti riservati
Dimensione 382.42 kB
Formato Adobe PDF
382.42 kB Adobe PDF   Richiedi una copia

I documenti in FLORE sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/652762
Citazioni
  • ???jsp.display-item.citation.pmc??? ND
  • Scopus 11
  • ???jsp.display-item.citation.isi??? 10
social impact