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The effects of poly(ethylene glycol) on the solution structure of human serum albumin
Author(s) -
Ragi C.,
SedaghatHerati M. R.,
Ouameur A. Ahmed,
TajmirRiahi H. A.
Publication year - 2005
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.20281
Subject(s) - chemistry , ethylene glycol , human serum albumin , serum albumin , human albumin , polymer chemistry , albumin , ethylene , organic chemistry , chromatography , biochemistry , catalysis
Protein physical and chemical properties can be altered by polymer interaction. The presence of several high affinity binding sites on human serum albumin (HSA) makes it a possible target for many organic and polymer molecules. This study was designed to examine the interaction of HSA with poly(ethylene glycol) (PEG) in aqueous solution at physiological conditions. Fourier transform infrared, ultraviolet‐visible, and CD spectroscopic methods were used to determine the polymer binding mode, the binding constant, and the effects of polymer complexation on protein secondary structure. The spectroscopic results showed that PEG is located along the polypeptide chains through H‐bonding interactions with an overall affinity constant of K = 4.12 × 10 5 M −1 . The protein secondary structure showed no alterations at low PEG concentration (0.1 m M ), whereas at high polymer content (1 m M ), a reduction of α‐helix from 59 (free HSA) to 53% and an increase of β‐turn from 11 (free HSA) to 22% occurred in the PEG–HSA complexes (infrared data). The CDSSTR program (CD data) also showed no major alterations of the protein secondary structure at low PEG concentrations (0.1 and 0.5 m M ), while at high polymer content (1 m M ), a major reduction of α‐helix from 69 (free HSA) to 58% and an increase of β‐turn from 7 (free HSA) to 18% was observed. 2005 Wiley Periodicals, Inc. Biopolymers 78: 231–236, 2005