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Glucose-induced structural changes and anomalous diffusion of elastin.

Debajyoti De1, Nisha Pawar1, Amar Nath Gupta1

  • 1Department of Physics, Indian Institute of Technology Kharagpur, W.B. 721302, India.

Colloids and Surfaces. B, Biointerfaces
|January 17, 2020
PubMed
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Glucose alters elastin structure and properties, impacting tissue elasticity. Elevated glucose levels induce significant changes, potentially explaining its role in skin aging.

Keywords:
Anomalous diffusionElastinGlucoseITTβ-sheet

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Area of Science:

  • Biophysics
  • Biomaterials Science
  • Protein Chemistry

Background:

  • Elastin, a key protein in elastic fibers, provides essential elasticity to tissues.
  • Understanding elastin's response to glucose is crucial for comprehending its role in aging and disease.
  • Altered glucose metabolism is implicated in age-related tissue degeneration.

Purpose of the Study:

  • To investigate the effects of varying glucose concentrations on the transport, viscoelastic, and structural properties of elastin.
  • To elucidate the molecular mechanisms underlying glucose-induced changes in elastin.
  • To correlate these structural changes with potential implications in age-related skin conditions.

Main Methods:

  • Multi-technique approach combining laser light scattering, rheology, and Fourier-transform infrared spectroscopy (FTIR).
  • Analysis of elastin's diffusion constant, inverse temperature transition, secondary structure content, and stiffness (Flory characteristic ratio).
  • Systematic variation of glucose concentration (X = [gluc]/[elastin]) to assess dose-dependent effects.

Main Results:

  • Laser light scattering revealed anomalous elastin behavior (β <0.6), with diffusion decreasing by 40% at high glucose (X>10).
  • Rheology demonstrated an inverse temperature transition at 40°C, shifting to lower temperatures with increasing glucose.
  • FTIR showed glucose favors β-sheet formation at low concentrations (X<10) but promotes β-turns and γ-turns over β-sheets and α-helices at high concentrations (X>10) due to crowding effects.
  • Protein stiffness, measured by Flory characteristic ratio, increased with glucose concentration.

Conclusions:

  • Glucose significantly alters elastin's structural and dynamic properties, including diffusion, thermal stability, and secondary structure.
  • High glucose concentrations induce protein crowding, leading to changes in secondary structure and increased stiffness.
  • These glucose-induced modifications of elastin may contribute to age-related skin issues and tissue degeneration.