In vitro formation and aggregation of heterotypic collagen I and III fibrils

Holger Notbohm*, Stephan Mosler, Peter K. Müller, Jürgen Brinckmann

*Corresponding author for this work
26 Citations (Scopus)


In vitro fibrillogenesis of solutions containing pepsin digested and acid soluble collagens I and III from human and bovine skin were investigated by turbidity-time measurements, dark-field and electron microscopy. The maximum turbidity of these solutions exhibited inversely proportional dependence on the collagen III content. Self-assembly was accelerated by collagen III. As a measure of mass per unit length, the maximum turbidity shows a mean decrease of 88% when comparing the absorbance at 313 nm for 0% and 50% collagen III in a composite solution of acid extracted collagen. In contrast to these findings, the diameter of fibrils from acid extracted fetal calf skin with 50% collagen III, determined from electron micrographs, was only 23% smaller than for pure collagen I. Correspondence with investigations on in vitro fibrillogenesis with dark-field microscopy and electron microscopy, this phenomenon apparently derives from the bundling of fibrils. This may be interpreted to mean that bundling of fibrils is already suppressed at low collagen III concentrations. A comparison of acid and pepsin extracted fetal calf skin yielded similar behaviour of collagen I and III mixtures, even though the pepsin extract displayed a turbidity reduction that was about 25% less than the acid extract. For pepsin digested collagen from human and bovine skin, differences were found for maximum turbidity and the ability to form bundles decreasing with the biological age of the donor.

Original languageEnglish
JournalInternational Journal of Biological Macromolecules
Issue number5
Pages (from-to)299-304
Number of pages6
Publication statusPublished - 01.01.1993

Research Areas and Centers

  • Academic Focus: Center for Infection and Inflammation Research (ZIEL)


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