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Related Concept Videos

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Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
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Proteins perform many mechanical functions in a cell. These proteins can be classified into two general categories- proteins that generate mechanical forces and proteins that are subjected to mechanical forces. Proteins providing mechanical support to the structure of the cell, such as keratin, are subjected to mechanical force, whereas proteins involved in cell movement and transport of molecules across cell membranes, such as an ion pump, are examples of generating mechanical force. 
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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
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Introducing Shear Stress in the Study of Bacterial Adhesion
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Shear-induced rotation enhances protein adsorption.

Zhengfu Zhang1, Kaixuan Lyu2, Bo Peng2

  • 1State Key Laboratory of Polymer Physics and Chemistry, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Jilin, Changchun 130022, PR China; School of Applied Chemistry and Engineering, University of Science and Technology of China, Hefei, Anhui 230026, PR China.

Colloids and Surfaces. B, Biointerfaces
|January 12, 2025
PubMed
Summary

Shear flow significantly increases protein adsorption rates at interfaces by enhancing rotational diffusion, not by causing desorption. This effect is concentration-dependent and observed for multiple plasma proteins.

Keywords:
Molecular dynamics simulationsProtein adsorptionShear rateSingle-molecule tracking

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Area of Science:

  • Biophysics
  • Surface Science
  • Fluid Dynamics

Background:

  • Theoretical models suggested shear promotes protein desorption.
  • Observing shear effects on individual protein adsorption/desorption is challenging due to aggregation.
  • Understanding shear flow's impact on protein adsorption kinetics at interfaces is crucial.

Purpose of the Study:

  • To investigate how shear flow influences the adsorption kinetics of plasma proteins at solid-liquid interfaces.
  • To determine if shear stress triggers protein desorption.
  • To elucidate the mechanisms behind shear-induced changes in adsorption rates.

Main Methods:

  • Employed high-throughput single-molecule tracking.
  • Utilized molecular dynamics simulations (coarse-grained and all-atom).
  • Conducted systematic analysis combining control experiments.

Main Results:

  • Shear stress (0–10^3 s^-1) did not induce protein desorption.
  • Observed a significant increase (up to two orders of magnitude) in adsorption rate constants (k_a) in the dilute limit.
  • Shear-induced increase in k_a diminished with increasing protein concentration, consistent across different proteins and surfaces.

Conclusions:

  • Shear flow enhances protein adsorption rates, contrary to some theoretical predictions.
  • The primary mechanism is enhanced protein rotational diffusion, increasing favorable surface interactions.
  • Findings are consistent for human serum albumin, immunoglobulin G, and fibrinogen on two surfaces.