2007
DOI: 10.1529/biophysj.106.094284
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Electrostatic Interactions Modulate the Conformation of Collagen I

Abstract: The pH- and electrolyte-dependent charging of collagen I fibrils was analyzed by streaming potential/streaming current experiments using the Microslit Electrokinetic Setup. Differential scanning calorimetry and circular dichroism spectroscopy were applied in similar electrolyte solutions to characterize the influence of electrostatic interactions on the conformational stability of the protein. The acid base behavior of collagen I was found to be strongly influenced by the ionic strength in KCl as well as in Ca… Show more

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Cited by 104 publications
(100 citation statements)
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References 65 publications
(101 reference statements)
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“…On the other hand, KCl addition leads to substantially lower Young's moduli (Figure 6b), even though other reports have also suggested that K + promotes collagen aggregation. 31 The changes we observe with the addition of CaCl 2 and KCl contrast with the minimal effect that similar concentrations of NaCl have on stiffness (Figure 6c). …”
Section: Correlating Mechanical Stiffness With Fibril Contentmentioning
confidence: 74%
“…On the other hand, KCl addition leads to substantially lower Young's moduli (Figure 6b), even though other reports have also suggested that K + promotes collagen aggregation. 31 The changes we observe with the addition of CaCl 2 and KCl contrast with the minimal effect that similar concentrations of NaCl have on stiffness (Figure 6c). …”
Section: Correlating Mechanical Stiffness With Fibril Contentmentioning
confidence: 74%
“…Adsorbing collagen to the PDMS surface by hydrophobic interactions possibly modulates the correct positioning of the glycine residues in the triple helix, thereby producing a collagen conformation that mediates only limited cell adhesion. Moreover, ionic strength has been described to modulate the collagen structure by shifting its isoelectric point [55]. Each polypeptide chain of collagen type I contains a high amount (15-20%) of ionizable residues [56], rendering electrostatic interactions important for the stability of the triple helix.…”
Section: Discussionmentioning
confidence: 99%
“…For example, an increase of the ionic strength with KCl from 10 -4 to 10 -2 M shifts the isoelectric point of the collagen from pH 7.5 to 5.3. A similar increase of the ionic strength in CaCl 2 solutions shifts the pI of the same protein from 7.5 to above pH 9 (Freudenberg et al 2007). Actually, the isoelectric points of native proteins under in vivo conditions cannot be estimated on the basis of in vitro experiments or calculated on the basis of primary sequences of proteins.…”
Section: Introductionmentioning
confidence: 89%