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Antithrombin stabilisation by sulfated carbohydrates correlates with anticoagulant activity

DOI: 10.1039/c3md00048f DOI Help

Authors: Marcelo Andrade De Lima (Universidade Federal de São Paulo) , Ashley Hughes (Diamond Light Source; University of Liverpool) , Noemi Veraldi (Istituto di Ricerche Chimiche e Biochimiche “G. Ronzoni”) , Timothy Rudd (University of Liverpool) , Rohanah Hussain (Diamond Light Source) , Adriana Brito (Universidade Federal de São Paulo (UNIFESP)) , Suely Chavante (Universidade Federal do Rio Grande do Norte) , Ivarne Tersariol (Universidade Federal de São Paulo (UNIFESP)) , Giuliano Siligardi (Diamond Light Source) , Helena B. Nader (Universidade Federal de São Paulo (UNIFESP)) , Edwin Yates (University of Liverpool)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Medchemcomm

State: Published (Approved)
Published: April 2013

Abstract: Thermal stabilisation of native antithrombin-III (AT), determined using differential scanning fluorimetry, correlated with the anticoagulant activity of heparin and heparin-related saccharides. Similar conformational changes were induced in native AT by a variety of active and inactive heparin-related sulfated carbohydrates, measured in solution using synchrotron radiation circular dichroism, and their anticoagulant activities. Measurement of native AT stabilisation provides a convenient assay for prospective anticoagulants and represents an additional parameter by which to compare biosimilar heparins.

Subject Areas: Chemistry, Medicine

Instruments: B23-Circular Dichroism

Added On: 09/04/2013 10:19

Discipline Tags:

Biochemistry Chemistry Biophysics Life Sciences & Biotech

Technical Tags:

Spectroscopy Circular Dichroism (CD)