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Related Concept Videos

Fibril-associated Collagen01:11

Fibril-associated Collagen

Fibril-associated collagens are a type of collagens present in the extracellular matrix with interrupted triple helices or FACIT (Fibril-associated collagens interrupted triple-helices). FACIT help connect and attach the collagen fibrils with each other as well as with other proteins of the extracellular matrix.
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...
IR Frequency Region: Fingerprint Region01:03

IR Frequency Region: Fingerprint Region

IR spectra are divided into two main regions: the diagnostic region and the fingerprint region. The diagnostic region of the spectrum lies above 1500 cm−1. The absorptions resulting from single-bond vibrations of the N–H, C–H, and O–H stretch at higher wavenumbers and appear on the left side of the spectrum. The stretching absorptions of the C≡C and C≡N occur between 2100–2300 cm−1. In contrast, those arising from stretching absorptions of the C=O, C=N, and C=C occur between 1600–1850 cm−1.
The...
Type IV Collagen of Basal Lamina01:05

Type IV Collagen of Basal Lamina

Type IV collagen is a 400 nm long, network-forming collagen that acts as a barrier between the epithelial and endothelial cells. Type IV collagen  forms the backbone of the basement membrane by scaffolding with laminin, entactin, proteoglycans, and fibronectin. Apart from rendering structural support to the basement membrane, it also helps entail signaling potentials necessary for both pathological and physiological functions.
A type IV collagen molecule has six alpha chains which can exist in...
Collagens are the Major Structural Proteins of ECM01:13

Collagens are the Major Structural Proteins of ECM

Three main types of fibers are secreted by fibroblasts: collagen fibers, elastic fibers, and reticular fibers. Collagen fiber is made from fibrous protein subunits linked together to form a long, straight fiber. Collagen fibers, while flexible, have great tensile strength, resist stretching, and give ligaments and tendons their characteristic resilience and strength. These fibers hold connective tissues together, even during the body's movement.
Connective tissue proper includes loose...
Fibrous Proteins00:55

Fibrous Proteins

Fibrous proteins are either long and narrow proteins or assemble to form long and thin structures. They contain repetitive units and usually consist of either alpha helices or beta sheets and, in rare cases, a mix of both. The amino acids in the primary structure often consist of repeating amino acid sequences. The role of fibrous proteins is primarily structural. Many are located in the extracellular matrix and are present in connective tissues to impart strength and joint mobility. They are...
Infrared (IR) Spectroscopy: Overview01:09

Infrared (IR) Spectroscopy: Overview

When electromagnetic radiation passes through a material, atoms or molecules transition from a lower to a higher energy state by absorbing radiation corresponding to the energy difference between the two states. The absorption of infrared (IR) radiation causes transitions between vibrational energy levels in a molecule. Therefore, IR spectroscopy is a useful analytical tool for determining the molecular structure of molecules.
Different compounds display unique properties due to their...

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Related Experiment Video

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Multimodal Nonlinear Hyperspectral Chemical Imaging Using Line-Scanning Vibrational Sum-Frequency Generation Microscopy
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Collagen types analysis and differentiation by FTIR spectroscopy.

Karima Belbachir1, Razia Noreen, Gilles Gouspillou

  • 1Université Victor Segalen Bordeaux 2, 146 rue Léo Saignat, 33076, Bordeaux-Cedex, France.

Analytical and Bioanalytical Chemistry
|August 18, 2009
PubMed
Summary
This summary is machine-generated.

Fourier-transform infrared (FTIR) spectroscopy effectively distinguishes between five collagen types. This advancement offers new possibilities for molecular histology and disease diagnosis by analyzing collagen biodistribution.

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Quantifying Fibrillar Collagen Organization with Curvelet Transform-Based Tools

Published on: November 11, 2020

Area of Science:

  • Biochemistry
  • Spectroscopy
  • Histology

Background:

  • Abnormal collagen network formation is implicated in numerous organ pathologies.
  • Current analytical methods for collagen biodistribution are limited.
  • Collagen types I, III, IV, V, and VI are crucial components of connective tissues.

Purpose of the Study:

  • To investigate the utility of Fourier-transform infrared (FTIR) spectroscopy for analyzing and classifying different collagen types.
  • To establish a robust method for differentiating between five key collagen types based on their spectral properties.

Main Methods:

  • Analysis of 30 FTIR spectra for each of the five collagen types (I, III, IV, V, VI).
  • Utilized four specific spectral intervals: Amide I (1,700-1,600 cm⁻¹), CH₂/CH₃ absorptions (1,480-1,350 cm⁻¹), Amide III (1,300-1,180 cm⁻¹), and carbohydrate moieties (1,100-1,005 cm⁻¹).
  • Employed curve fitting analysis and multivariate statistical methods (MANOVA, Dunnett's T3 post hoc test) for submolecular justification and validation.

Main Results:

  • A robust classification of FTIR spectra was achieved for all five collagen types.
  • Each of the four spectral intervals contained highly discriminant absorption bands between collagen types (p < 0.01).
  • Statistical analysis confirmed significant differences in spectral features across collagen types (p < 0.05).

Conclusions:

  • FTIR spectroscopy provides a reliable method for differentiating between major collagen types.
  • The findings support FTIR spectroscopy and imaging as valuable tools for molecular histology.
  • This technique holds significant potential for advancing diagnostic methods in various pathologies.