TY - JOUR
T1 - Effect of buffer on heparin binding and sensing in competitive aqueous media
AU - Chan, Ching Wan
AU - Smith, David Kelham
N1 - © 2016 informa uK limited, trading as taylor & Francis Group. This is an author-produced version of the published paper. Uploaded in accordance with the publisher’s self-archiving policy. Further copying may not be permitted; contact the publisher for details.
PY - 2017
Y1 - 2017
N2 - Although buffer-specific effects on molecular recognition are known in biological science, they remain rare in supramolecular chemistry. The binding between a cationic dye, Mallard Blue (MalB), and polyanionic heparin in aqueous NaCl (150 mM) is studied in three commonly-used buffers (Tris-HCl, HEPES, Phosphate, each 10 mM). Although MalB has a very similar UV-Vis spectrum in each buffer, the sensory response towards heparin was different in each case. This can be ascribed to differences in the complex formed. In Tris-HCl which has the least competitive chloride counter-anions, MalB exhibits a hypsochromic shift of 25 nm, assigned to strong binding and aggregation of the dye on heparin. In more competitive HEPES, containing a sulfonate anion, there is weaker binding and less aggregation of MalB along the heparin; the hypsochromic shift is only 15 nm. In phosphate buffer, MalB can interact quite strongly with buffer phosphate anions; although heparin binding is still observed, the hypsochromic shift associated with dye aggregation is only 5 nm. As such, specific buffer interactions with the MalB-heparin complex mediate host-guest binding and sensing. Buffer choice must be made carefully in studies of molecular recognition – we would caution against using phosphate and sulfonate containing buffers when studying electrostatic binding.
AB - Although buffer-specific effects on molecular recognition are known in biological science, they remain rare in supramolecular chemistry. The binding between a cationic dye, Mallard Blue (MalB), and polyanionic heparin in aqueous NaCl (150 mM) is studied in three commonly-used buffers (Tris-HCl, HEPES, Phosphate, each 10 mM). Although MalB has a very similar UV-Vis spectrum in each buffer, the sensory response towards heparin was different in each case. This can be ascribed to differences in the complex formed. In Tris-HCl which has the least competitive chloride counter-anions, MalB exhibits a hypsochromic shift of 25 nm, assigned to strong binding and aggregation of the dye on heparin. In more competitive HEPES, containing a sulfonate anion, there is weaker binding and less aggregation of MalB along the heparin; the hypsochromic shift is only 15 nm. In phosphate buffer, MalB can interact quite strongly with buffer phosphate anions; although heparin binding is still observed, the hypsochromic shift associated with dye aggregation is only 5 nm. As such, specific buffer interactions with the MalB-heparin complex mediate host-guest binding and sensing. Buffer choice must be made carefully in studies of molecular recognition – we would caution against using phosphate and sulfonate containing buffers when studying electrostatic binding.
U2 - 10.1080/10610278.2016.1234711
DO - 10.1080/10610278.2016.1234711
M3 - Article
SN - 1029-0478
VL - 29
SP - 688
EP - 695
JO - Supramolecular Chemistry
JF - Supramolecular Chemistry
ER -