Controlled self-assembly of collagen fibrils by an automated dialysis system

J Biomech Eng. 2006 Oct;128(5):792-6. doi: 10.1115/1.2264392.

Abstract

In vitro self-assembled collagen fibrils form a variety of different structures during dialysis. The self-assembly is dependent on several parameters, such as concentrations of collagen and alpha1-acid glycoprotein, temperature, dialysis time, and the acid concentration. For a detailed understanding of the assembly pathway and structural features like banding pattern or mechanical properties it is necessary to study single collagen fibrils. In this work we present a fully automated system to control the permeation of molecules through a membrane like a dialysis tubing. This allows us to ramp arbitrary diffusion rate profiles during the self-assembly process of macromolecules, such as collagen. The system combines a molecular sieving method with a computer assisted control system for measuring process variables. With the regulation of the diffusion rate it is possible to control and manipulate the collagen self-assembly process during the whole process time. Its performance is demonstrated by the preparation of various collagen type I fibrils and native collagen type II fibrils. The combination with the atomic force microscope (AFM) allows a high resolution characterization of the self-assembled fibrils. In principle, the represented system can be also applied for the production of other biomolecules, where a dialysis enhanced self-assembly process is used.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization / methods*
  • Equipment Design
  • Equipment Failure Analysis
  • Fibrillar Collagens / chemistry*
  • Fibrillar Collagens / ultrastructure*
  • Microdialysis / instrumentation*
  • Microdialysis / methods
  • Multiprotein Complexes / chemistry
  • Multiprotein Complexes / ultrastructure

Substances

  • Fibrillar Collagens
  • Multiprotein Complexes