FT-IR approaches on amyloid fibril structure

Hiramatsu, Hirotsugu; Kitagawa, Teizo

doi:10.1016/j.bbapap.2005.07.008

Cited by 122 publications

(112 citation statements)

References 71 publications

Supporting

Mentioning

108

Contrasting

Unclassified

Order By: Relevance

“…The secondary structure of proteins associated with the "β-sheet" which is the common structure of the amyloid fibrils. Generally, FTIR spectra of the proteins give the strong absorption band in the 1700-1600 cm -1 region (amide I) indicate the C=O stretching mode of the peptide chain [30][31][32]. In this amide I region (1700-1600 cm -1 ), the band appears at 1660-1640 cm -1 for α-helix and random coils and also band at 1640-1620 cm -1 appears for β-sheet.…”

Section: Resultsmentioning

confidence: 99%

FTIR Spectroscopic Study of Heat-Induced β-Lactoglobulin Solution under Flow Field

Sharma¹,

Furusawa²,

Fukui³

et al. 2018

Asian J. Chem.

View full text Add to dashboard Cite

Effect of stirring on the secondary structure of amyloid fibrillogenesis of β-lactoglobulin (βLG) at pH 2 and at pH 7 with and without glucose was studied. Fibrillogenesis at pH 2 was carried out by heating the 4w % β-lactoglobulin and at pH 7 by heating the 0.30 mM β-lactoglobulin in 0.1 M, pH 7 sodium phosphate buffer solution with and without glucose (37.5 mM) for 24 h under stirring (250 and 474 rpm) conditions. For control samples, β-lactoglobulin solutions were incubated under unstirred condition at pH 2 and pH 7. The secondary structure of the amyloid fibrils which corresponds the β-sheet structure was studied by using Fourier transform infrared (FTIR) spectroscopy revealed that the stirring does not affect the secondary structure of the β-lactoglobulin fibrils at pH 2 as well as pH 7 with and without glucose.

show abstract

Section: Resultsmentioning

confidence: 99%

FTIR Spectroscopic Study of Heat-Induced β-Lactoglobulin Solution under Flow Field

Sharma¹,

Furusawa²,

Fukui³

et al. 2018

Asian J. Chem.

View full text Add to dashboard Cite

show abstract

“…3, the resultant IR spectra provided an amide I absorption band at 1645-44 cm -1 and an amide II absorption band at 1541-35 cm -1 . Absorption bands at 1650-40 and 1550-20 are characteristic of -helical structure [18,19] and thus the Phe peptides immobilized on CSP1-3 were assumed to be mainly in the -helical state.…”

Section: Resultsmentioning

confidence: 99%

“…The secondary structure of a peptide depends on its chain length [15] and variation in secondary structure could impact on enantioselectivity. An IR spectra is widely used to estimate the conformation of peptides and proteins from their amide I and II absorption bands [12,13,[18][19][20][21]. IR measurement on CSP1-3, initially dispersed in the mobile phase for 12 h and then dried in vacuo at ambient temperature, was carried out.…”

Section: Resultsmentioning

confidence: 99%

Preparation and characterization of poly(l-phenylalanine) chiral stationary phases with varying peptide length

Ohyama¹,

Oyamada²,

Kishikawa³

et al. 2008

Journal of Chromatography A

View full text Add to dashboard Cite

Three new chiral stationary phases with different lengths of L-phenylalanine peptide were prepared by solid-phase synthesis with Boc-L-phenylalanine on silica. The effect of phenylalanine peptide length on enantioselectivity was studied. The best separation of R/S-warfarin was achieved by the chiral stationary phase with intermediate peptide length. These stationary phases were found to exist mainly in -helical conformation by using FT-IR spectra. The end-capping reagents for the N-terminus of the peptide were also evaluated.3

show abstract

“…During the last years the use of Fourier transform infrared (FTIR) spectroscopy has dramatically expanded and become crucial for monitoring the structure of proteins and to detect the presence of β-sheet secondary structure. Typically, the sample is examined before and after aggregation and an increase in β-sheet secondary structure is observed upon amyloid fibril formation [25][26][27] . Moreover, the kinetics of aggregation have been monitored by UV-visible spectroscopy (Fig.…”

Section: Preparation and Characterisation Of Protein Samplesmentioning

confidence: 99%

Investigation of protein aggregation dynamics with a Bloch surface wave sensor

Paeder¹,

Santi²,

Musi³

et al. 2011

Novel Biophotonic Techniques and Applications

View full text Add to dashboard Cite

We present a study of the dynamics of protein aggregation using a common path heterodyne Bloch surface wave sensing scheme. We demonstrate the ability to detect, during thermal incubation, the early events linked to the aggregation of proteins related to conformational diseases. Alzheimer's amyloid-β 1-42 is used to demonstrate the efficiency of the method. A model based on elementary interactions is shown to describe accurately the aggregation process. The described sensing scheme is sensitive to the early events of the aggregation process. is hence proposed as a method for the detection of early stages of the evolution of conformational diseases.

show abstract

FT-IR approaches on amyloid fibril structure

Cited by 122 publications

References 71 publications

FTIR Spectroscopic Study of Heat-Induced β-Lactoglobulin Solution under Flow Field

FTIR Spectroscopic Study of Heat-Induced β-Lactoglobulin Solution under Flow Field

Preparation and characterization of poly(l-phenylalanine) chiral stationary phases with varying peptide length

Investigation of protein aggregation dynamics with a Bloch surface wave sensor

Contact Info

Product

Resources

About