Electrostatic effects in collagen fibril formation

Svetlana Morozova, Murugappan Muthukumar

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

Abstract

Using light scattering and Atomic Force Microscopy techniques, we have studied the kinetics and equilibrium scattering intensity of collagen association, which is pertinent to the vitreous of the human eye. Specifically, we have characterized fibrillization dependence on pH, temperature, and ionic strength. At higher and lower pH, collagen triple helices remain stable in solution without fibrillization. At physiological pH, fibrillization occurs and the fibril growth is slowed upon either an increase in ionic strength or a decrease in temperature. The total light scattering with respect to ionic strength is non-monotonic in these conditions as a result of a competing dependence of fibril concentration and size on ionic strength. Fibril concentration is the highest at lower ionic strengths and rapidly decays for higher ionic strengths. On the other hand, fibril size is larger in solutions with higher ionic strength. We present a theoretical model, based on dipolar interactions in solutions, to describe the observed electrostatic nature of collagen assembly. At extreme pH values, either very low or very high, collagen triple helices carry a large net charge of the same sign preventing their assembly into fibrils. At intermediate pH values, fluctuations in the charge distribution of the collagen triple helices around roughly zero net charge lead to fibrillization. The growth kinetics of fibrils in this regime can be adequately described by dipolar interactions arising from charge fluctuations.

Original languageEnglish (US)
Article number163333
JournalJournal of Chemical Physics
Volume149
Issue number16
DOIs
StatePublished - Oct 28 2018

Bibliographical note

Funding Information:
Acknowledgment is made to the National Science Foundation (Award No. 1504265) and Air Force Office of Scientific Research (Grant No. FA9550-17-1-0160).

Funding Information:
National Science Foundation (Award No. 1504265) and Air Force Office of Scientific Research (Grant No. FA9550-17-1-0160).

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