tSurface functionalization by layers of hydrophobins, amphiphilic proteins produced by fungi offers apromising and green strategy for fabrication of biomedical and bioanalytical devices. The layering pro-cess of the Vmh2 hydrophobin from Pleurotus ostreatus on Teflon membrane has been investigated byAttenuated Total Reflection Fourier Transform Infrared (ATR FT-IR) spectroscopy. In particular, proteinlayers obtained with hydrophobin purified with two different procedures and in various coating condi-tions have been examined. The layers have been characterized by quantifying the amide I and amide IIband area together with the lipid/amide ratio and carbohydrate/amide ratio. This characterization can bevery useful in evaluating the best purification strategy and coating conditions. Moreover the analysis ofthe secondary structure of the layered protein using the deconvolution procedure of amide I band indi-cate the prevalent contribution from -sheet state. The results inferred by infrared spectroscopy havebeen also confirmed by scanning electron microscopy imaging.

ATR FT-IR spectroscopy on Vmh2 hydrophobin self-assembled layers for Teflon membrane bio-functionalization

GRAVAGNUOLO, ALFREDO MARIA;LONGOBARDI, SARA;GIARDINA, PAOLA;LEPORE, MARIA
2015

Abstract

tSurface functionalization by layers of hydrophobins, amphiphilic proteins produced by fungi offers apromising and green strategy for fabrication of biomedical and bioanalytical devices. The layering pro-cess of the Vmh2 hydrophobin from Pleurotus ostreatus on Teflon membrane has been investigated byAttenuated Total Reflection Fourier Transform Infrared (ATR FT-IR) spectroscopy. In particular, proteinlayers obtained with hydrophobin purified with two different procedures and in various coating condi-tions have been examined. The layers have been characterized by quantifying the amide I and amide IIband area together with the lipid/amide ratio and carbohydrate/amide ratio. This characterization can bevery useful in evaluating the best purification strategy and coating conditions. Moreover the analysis ofthe secondary structure of the layered protein using the deconvolution procedure of amide I band indi-cate the prevalent contribution from -sheet state. The results inferred by infrared spectroscopy havebeen also confirmed by scanning electron microscopy imaging.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11588/613376
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