Intermolecular Interactions in Collagen Self-Assembly as Revealed by Fourier Transform Infrared Spectroscopy

Jakobsen, R. J.; Brown, L. L.; Hutson, Timothy B.; Fink, David J.; Veis, Arthur

doi:10.1126/science.6857249

Cited by 92 publications

(37 citation statements)

References 12 publications

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“…The frequency of the amide II peak also decreased. This trend was similar to that seen in a previous study in which the amide peak frequency downshift was observed when full-length collagen forms fibrils by increasing the temperature of the collagen solution, [26] suggesting that the film formed by slow evaporation of NATCOL peptide solution contained similar collagen fibrillar structure. However, no changes in the position of Amide I peak were observed for films formed from NATCOL by fast evaporation, indicating fast evaporation tends to prevent formation of ordered phases.…”

Section: Fourier Transformed Infrared Spectroscopysupporting

confidence: 87%

Hierarchical Assembly of Collagen‐Like Peptides in vitro Provides Structural Causes of Osteogenesis Imperfecta

Huang¹,

Cebe²,

Kaplan³

2009

Macromol. Rapid Commun.

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Collagen type I peptides, representative of native to disease states for the bone disease, Osteogenesis imperfecta, were studied with regard to self-assembly into triple helices and liquid crystalline mesophases. The purpose of the study was to establish insight into collagen mutations in terms of propagation of single chain defects up the scale of materials hierarchy, toward solid state fibril assemblies formed from collagen. Studies carried out in vitro demonstrated the value of this approach in establishing in vitro disease models, as the degree of collagen disruption could be recapitulated by the point mutations to show major impact on macroscopic features. Fourier transform infrared spectroscopy, circular dichroism, atomic force microscopy and optical ellipsometry were used to assess the structural and morphological changes at the various length scales post assembly. The results demonstrated that glycine to alanine to aspartic acid single substitutions in the collagen peptides progressively disrupted normal assembly, reflected in lower thermal stability, loss of triple helical structure and loss of mesophase formation. This approach can provide a basis upon which to study collagen biomaterial templates for controlled hydroxyapatite formation and changes in cell signaling related to bone remodeling, related to the severity of the disease.

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Section: Fourier Transformed Infrared Spectroscopysupporting

confidence: 87%

Hierarchical Assembly of Collagen‐Like Peptides in vitro Provides Structural Causes of Osteogenesis Imperfecta

Huang¹,

Cebe²,

Kaplan³

2009

Macromol. Rapid Commun.

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“…These amide bands are considered to be signatures which characterize peptide conformation. [16] Despite the general similarities, the spectra for the two types of fibrils exhibit some differences. The observed differences are mostly manifested in the positions of the characteristic amide bands.…”

Section: Resultsmentioning

confidence: 99%

Polymorphism of amyloid fibrils formed by a peptide from the yeast prion protein Sup35: AFM and Tip-Enhanced Raman Scattering studies

et al. 2016

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Aggregation of prion proteins is the cause of various prion related diseases. The infectious form of prions, amyloid fibrils, exist as multiple strains. The strains are thought to represent structurally different prion protein molecules packed into amyloid fibrils, but the knowledge on the structure of different types of aggregates is limited. Here we report on the use of AFM (Atomic Force Microscopy) and TERS (Tip-Enhanced Raman Scattering) to study morphological heterogeneity and access underlying conformational features of individual amyloid aggregates. Using AFM we identified morphology of amyloid fibrils formed by the peptide (CGNNQQNY) from the yeast prion protein Sup35 that is critically involved in the aggregation of the full protein. TERS results demonstrate that morphologically different amyloid fibrils are composed of a distinct set of conformations. Fibrils formed at pH 5.6 are composed of a mixture of peptide conformations (β-sheets, random coil and α-helix) while fibrils formed in pH~2 solution primarily have β-sheets. Additionally, peak positions in the amide III region of the TERS spectra suggested that peptides have parallel arrangement of β-sheets for pH~2 fibrils and antiparallel arrangement for fibrils formed at pH 5.6. We also developed a methodology for detailed analysis of the peptide secondary structure by correlating intensity changes of Raman bands in different regions of TERS spectra. Such correlation established that structural composition of peptides is highly localized with large contribution of unordered secondary structures on a fibrillar surface.

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“…18,23,24 Therefore, these spectral alterations together with the reduced amide III band in this study represented the imposed molecular interactions of Chi on Col, including depression of hydrogen bonding of Col self assembly and forming complexes with Col. However, the complete denaturation of Col did not occur in this study.…”

mentioning

confidence: 96%

Synthesis and evaluation of collagen–chitosan–hydroxyapatite nanocomposites for bone grafting

Wang

Tan

et al. 2008

J Biomedical Materials Res

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Incorporation of hydroxyapatite (HA) into the matrix of collagen (Col) and chitosan (Chi) by in situ synthesis was introduced to prepare nanocomposites. Structural investigations of the pure Col-Chi mixture validated the influence of Chi on Col assembly, but the molecular interactions between Col and Chi was partially depressed during the intervention of in situ HA synthesis, as revealed by FTIR and DSC analyses. A series of Col-Chi-HA (CCHA) nanocomposites with varying HA content were thereby prepared by a sequential method, involving in situ synthesis in the Col-Chi system, then gelling at 25 degrees C and subsequently washing the resultant elastic gel followed by dehydration consolidation. The structural characteristics and biological properties of the dehydrated CCHA nanocomposites were further evaluated by using XRD, FTIR, TG, and SEM analyses and the osteoblast culture experiment. Formation of a well integrated microstructure of organic fibers (ca. 90 nm in size) and dense matrix including inorganic aggregates (less than 30 nm in size) was found in these nanocomposites. Rat Ros 17/2.8 Osteoblasts proliferated and attached well on the surface of both CCHA nanocomposite and Col-Chi mixture. These results indicated that in situ HA synthesis in the Col-Chi system provided a feasible route for bone grafting nanocomposites.

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Intermolecular Interactions in Collagen Self-Assembly as Revealed by Fourier Transform Infrared Spectroscopy

Cited by 92 publications

References 12 publications

Hierarchical Assembly of Collagen‐Like Peptides in vitro Provides Structural Causes of Osteogenesis Imperfecta

Hierarchical Assembly of Collagen‐Like Peptides in vitro Provides Structural Causes of Osteogenesis Imperfecta

Polymorphism of amyloid fibrils formed by a peptide from the yeast prion protein Sup35: AFM and Tip-Enhanced Raman Scattering studies

Synthesis and evaluation of collagen–chitosan–hydroxyapatite nanocomposites for bone grafting

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