FT-IR studies of sickle hemoglobin interaction with phosphatidylserine | Zendy

Hao OuYang | Zendy; David J. Moore | Zendy; Richard H. Sills | Zendy; Richard Mendelsohn | Zendy

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FT-IR studies of sickle hemoglobin interaction with phosphatidylserine

Author(s) -

Hao OuYang,

David J. Moore,

Richard H. Sills,

Richard Mendelsohn

Publication year - 2004

Publication title -

journal of spectroscopy

Language(s) - English

Resource type - Journals

eISSN - 2314-4920

pISSN - 2314-4939

DOI - 10.1155/2004/805318

Subject(s) - hemoglobin , phosphatidylserine , chemistry , phospholipid , fourier transform infrared spectroscopy , crystallography , biochemistry , chemical engineering , membrane , engineering

The interaction of dilauroylphosphatidylserine (DLPS) vesicles with both normal human hemoglobin (HbA) and hemoglobin from patients with sickle cell disease (HbS) has been investigated with FTIR spectroscopy. Changes in the con- formational order of the phospholipid chains were directly monitored via the acyl chain CH2 symmetric stretching mode frequencies. The hemoglobin oxygenation state was simultaneously monitored via the S-H stretching contour. The current study reveals that under oxygenated conditions, DLPS shows little interaction with either HbA or HbS. In contrast, deoxyHbS interacted with DLPS by abolishing the gel-liquid crystal phase transition.

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