ArticleEuropean biophysics journal : EBJ2003
Conformation of heparin studied with macromolecular hydrodynamic methods and X-ray scattering.
Article in European biophysics journal : EBJ, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 108 citations in OpenAlex.
- Solvent Models and Charge Scaling: Benchmarks for Molecular Dynamics of Glycosaminoglycans.The journal of physical chemistry. B · 2026Article
- Unravelling the molecular network structure of biohybrid hydrogels.Materials today. Bio · 2025Article
- The Role of Long-Range Non-Specific Electrostatic Interactions in Inhibiting the Pre-Fusion Proteolytic Processing of the SARS-CoV-2 S Glycoprotein by Heparin.Biomolecules · 2025Article
- Biological Polymers: Evolution, Function, and Significance.Accounts of chemical research · 2025Article
- Molecular architecture and platelet-activating properties of small immune complexes assembled on heparin and platelet factor 4.Communications biology · 2024Article
- Mapping the configurational landscape and aggregation phase behavior of the tau protein fragment PHF6.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Extension of the SUGRES-1P Coarse-Grained Model of Polysaccharides to Heparin.Journal of chemical theory and computation · 2023Article
- Solvent Model Benchmark for Molecular Dynamics of Glycosaminoglycans.Journal of chemical information and modeling · 2023Article
- Biocompatible Macroion/Growth Factor Assemblies for Medical Applications.Biomolecules · 2023Review
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- Structural Changes in Polymeric Gel Scaffolds Around the Overlap Concentration.Frontiers in chemistry · 2019Article
- Binding Kinetics and Lateral Mobility of HSV-1 on End-Grafted Sulfated Glycosaminoglycans.Biophysical journal · 2017Article
- Binding of the chemokine CXCL12α to its natural extracellular matrix ligand heparan sulfate enables myoblast adhesion and facilitates cell motility.Biomaterials · 2017Article
- Electrostatic Forces as Dominant Interactions Between Proteins and Polyanions: an ESI MS Study of Fibroblast Growth Factor Binding to Heparin Oligomers.Journal of the American Society for Mass Spectrometry · 2017Article
- Article
- Investigation of the heparin-thrombin interaction by dynamic force spectroscopy.Biochimica et biophysica acta · 2015Article
- Characterization of a multilayer heparin coating for biomolecule presentation to human mesenchymal stem cell spheroids.Biomaterials science · 2014Article
- DNA compaction induced by a cationic polymer or surfactant impact gene expression and DNA degradation.PloS one · 2014Article
- The solution structure of heparan sulfate differs from that of heparin: implications for function.The Journal of biological chemistry · 2013Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The hydrodynamic characteristics of heparin fractions in a 0.2 M NaCl solution have been determined. Experimental values varied over the following ranges: the sedimentation coefficient (at 20.0 degrees C), 1.3<s0x10(13)<3.2 s; the Gralen coefficient (sedimentation concentration-dependence parameter), 10<ks<70 cm3 g(-1); the translational diffusion coefficient, 3.9< D0x10(7)<15.4 cm2 s(-1); the intrinsic viscosity, 7.9<[eta]<40 cm3 g(-1). Combination of s0 with D0 using the Svedberg equation yielded molecular weights in the range 3.9<Mx10(-3)<37 g mol(-1). The value of the mass per unit length of the heparin molecule, ML, was determined using the theory of hydrodynamic properties of a weakly bending rod, giving ML=570 +/- 50 g nm(-1) mol(-1). The equilibrium rigidity, Kuhn segment length (A=9 +/- 2 nm) and hydrodynamic diameter (d=0.9 +/- 0.1 nm) of heparin were evaluated on the basis of the worm-like coil theory without the excluded volume effect, using the combination of hydrodynamic data obtained from fractions of different sizes. Small-angle X-ray scattering for three heparin fractions allowed an estimate for the cross-sectional radius of gyration as 0.43 nm; from the evolution with the macromolecule contour length of the radius of gyration, a value for the Kuhn segment length of 9 +/- 1 nm was obtained. A good correlation is thus observed for the conformational parameters of heparin from hydrodynamic and X-ray scattering data. These values describe heparin as a semi-rigid polymer, with an equilibrium rigidity that is essentially determined by a structural component, the electrostatic contribution being negligible in 0.2 M NaCl.
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