The use of Fourier transform-infrared (FTIR) and Raman spectroscopy (FTR) for the investigation of structural changes in wool fibre keratin after enzymatic treatment

Wojciechowska, Elżbieta; Rom, Monika; Włochowicz, A.; Wysocki, Marian; Wesełucha–Birczyńska, Aleksandra

doi:10.1016/j.molstruc.2004.03.044

Cited by 59 publications

(33 citation statements)

References 15 publications

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“…To analyze the amide I complex band, we accepted that the band with a maximum at 1651 cm −1 5, 6, 13, 18–23 represented the vibration of the α helix, the band with a maximum at 1677 cm −1 5, 6, 13, 19, 20 represented the β‐sheet structure, and the band at 1624 cm −1 was due to the β‐sheet parallel 18. Also, the band component observed at 1695 cm −1 was assigned to the amide group of the asparagine and glutamine side chains 13, 22…”

Section: Resultsmentioning

confidence: 99%

“…Microfibrils represent the crystalline part in the fiber structure, and they are surrounded by an amorphous matrix phase 4. Polypeptide macromolecules in microfibrils have a predominantly α‐helical conformation; however, some authors have stated that there is about a 40% β‐sheet content 5, 6. These are held together by intermolecular and intramolecular interactions such as hydrogen bonds, van der Waals interactions, some salt linkages and disulfide bonds (crosslinks) 1, 7, 8.…”

Section: Introductionmentioning

confidence: 99%

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Analysis of the contribution of the microfibrils and matrix to the deformation processes in wool fibers

Tsobkallo

Aksakal

Darvish

2012

J of Applied Polymer Sci

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In this study, the mechanical and structural characteristics of wool fibers were examined, and the contributions of the microfibrils and matrix to the deformation processes were analyzed. The experiments were carried out on single wool fibers. To understand the structural changes at different deformation levels, the wool fibers were treated with a complex mechanical regime. One of the most significant results from the mechanical tests was the estimation of the modulus of the matrix, which changed from 0.07 to 1.6 GPa during stretching. This result proves the proposal of the netlike structure of the matrix. On the basis of the obtained experimental data and the structural model, where the microfibrils and matrix play the role of a reinforcing phase and a filler, respectively, the rigidity of the microfibrils in the initial unstretched state was determined to be equal to about 20 GPa. The experimental data obtained from the Fourier transform infrared–attenuated total reflectance spectroscopy method proved the α–β conformational transition both in the yield and postyield regions and revealed the presence of the stable β form, which was not sensitive to stretching. © 2012 Wiley Periodicals, Inc. J Appl Polym Sci, 2012

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Analysis of the contribution of the microfibrils and matrix to the deformation processes in wool fibers

Tsobkallo

Aksakal

Darvish

2012

J of Applied Polymer Sci

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“…The amide A band usually occurs at approx. 3286 cm −1 and the amide B band occurs at 3056-3075 cm −1 [27][28][29]. In Fig.…”

Section: Spectroscopic Investigation Of Coated Woolmentioning

confidence: 82%

Tyrosinase-Catalysed Coating of Wool Fibres With Different Protein-Based Biomaterials

Jus

Kokol

Guebitz

2009

Journal of Biomaterials Science, Polymer Edition

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The potential of tyrosinases to activate tyrosine residues of wool protein fibres for cross-linking with different materials like collagen, elastin and gelatine was assessed. Natural fibres like wool offer an excellent environment for the growth of micro-organisms when the conditions like moisture, oxygen and temperature are appropriate. Coating with collagen, a very useful biomaterial with bactericidal and fungicidal properties, could be used to improve the properties of wool-based materials, especially when applied in hygienically sensitive applications like in hospitals. Tyrosinases were shown to catalyse the oxidation of tyrosine residues in wool and wool hydrolysates as model substrates, as determined by UV-Vis spectroscopy. Structural differences of the surface were evident from the increase of the intensity in the NH bending and stretching regions in the spectra of NIR FT Raman analysis of the enzyme treated and grafted wool fibres. The durability of the coating was also shown by using FITC-labelled collagen that was bound to the wool fibres, even after severe washing. Additionally, antimicrobial properties were successfully imparted due to the collagen grafted on the wool fibres. The functional and mechanical properties of the treated wool fibres showed no significant changes.

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“…In order to understand the alterations in secondary structure of a protein as a consequence of SDS treatment, curve fitting of amide I band was carried out [39][40][41][42][43]. Figure 3 shows the curve fitting of amide I band for sample A where control root and tip samples are compared with the samples obtained after final SDS treatment.…”

Section: Ft-ir Atr Studymentioning

confidence: 99%

Effect of SDS on human hair: Study on the molecular structure and morphology

Singh

Umapathy

2010

Journal of Biophotonics

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This paper presents a model study to understand the effect of surfactants on the physicochemical properties of human hair. FT-IR ATR spectroscopy has been employed to understand the chemical changes induced by sodium dodecyl sulfate (SDS) on human scalp hair. In particular, the SDS induced changes in the secondary structure of protein present in the outer protective layer of hair, i.e. cuticle, have been investigated. Conformational changes in the secondary structure of protein were studied by curve fitting of the amide I band after every phase of SDS treatment. It has been found that SDS brings rearrangements in the protein backbone conformations by transforming β -sheet structure to random coil and β -turn. Additionally, AFM and SEM studies were carried out to understand the morphological changes induced on the hair surface. SEM and AFM images demonstrated the rupture and partial erosion of cuticle sublayers.

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The use of Fourier transform-infrared (FTIR) and Raman spectroscopy (FTR) for the investigation of structural changes in wool fibre keratin after enzymatic treatment

Cited by 59 publications

References 15 publications

Analysis of the contribution of the microfibrils and matrix to the deformation processes in wool fibers

Analysis of the contribution of the microfibrils and matrix to the deformation processes in wool fibers

Tyrosinase-Catalysed Coating of Wool Fibres With Different Protein-Based Biomaterials

Effect of SDS on human hair: Study on the molecular structure and morphology

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