Specific Binding Sites on Albumin

Sudlow, Gillian

doi:10.1016/b978-0-08-023768-8.52351-3

Cited by 74 publications

(114 citation statements)

References 0 publications

Supporting

Mentioning

110

Contrasting

Order By: Relevance

“…Furthermore, albumin on a1-AGP together accounted for only 30% of observed warfarin free fraction variance, implying that other factors are important determinants of variations in warfarin binding. The inverse relationship between diazepam and warfarin free fraction has been reported recently (Sellers et al, 1980) and seems to occur because diazepam and warfarin bind to albumin at two different sites with reciprocal modulations of binding affinity (Sudlow, 1979).…”

Section: Discussionmentioning

confidence: 98%

Variations in drug free fraction during alcohol withdrawal.

Sandor¹,

Naranjo²,

Khouw³

et al. 1983

Brit J Clinical Pharma

View full text Add to dashboard Cite

1 Free fractions of diazepam, propranolol and warfarin were determined in 15 male chronic alcoholics in alcohol withdrawal. 2 On admission the mean free fraction of diazepam was 25% above and propranolol 44% below the limits of normal range, while the mean warfarin free fraction was in high normal range. One week later mean free fraction of diazepam declined by 20% while propranolol and warfarin increased by 24% and 19% respectively (P < 0.05).3 Propranolol free fraction and a,-AGP concentrations were highly correlated (linear r = -0.83, P < 0.001). In contrast the sources of variation in diazepam and warfarin free fraction were more complex and less certain. 4 Statistically significant changes of drug free fractions in serum of chronic alcoholics were observed during alcohol withdrawal. The extent and direction of these changes differed for various classes of drugs and their potential causes appear to be quite different. 5 Clinically important changes in drug effect may be present acutely, within the dosing interval, as a result of altered drug binding. These are more likely when the clinical response is closely related to drug concentration and will occur within the dosing interval due to larger fluctuations in free drug concentration, even though the average free drug concentration will remain unchanged. 6 Total drug level changes will be observed during alcohol withdrawal even in absence of detectable changes of drug metabolism.

show abstract

Section: Discussionmentioning

confidence: 98%

Variations in drug free fraction during alcohol withdrawal.

Sandor¹,

Naranjo²,

Khouw³

et al. 1983

Brit J Clinical Pharma

View full text Add to dashboard Cite

show abstract

“…Sudlow (1978) carried out studies on specific binding sites on human albumin and found that the affinity of albumin for bilirubin at its primary site is so great as to make competition for binding by other ligands virtually impossible. However, changes in albumin conformation as a result of ligand binding have been frequently observed.…”

Section: Pooled Cord Serummentioning

confidence: 99%

The effect of semisynthetic penicillins on the binding of bilirubin by neonatal serum.

Friedman¹,

Lewis²

1980

Brit J Clinical Pharma

View full text Add to dashboard Cite

1. The effect of ampicillin, cloxacillin, flucloxacillin and sulphafurazole on bilirubin on bilirubin binding by pooled human umbilical cord serum and bovine serum albumin was studied in vitro using Sephadex gel filtration. 2. Sulphafurazole displaced bilirubin from binding; both cloxacillins displaced bilirubin from pooled cord serum but not bovine serum albumin. 4. No displacement of bilirubin by the cloxacillins from pooled cord serum could be detected at therapeutic plasma concentrations of these drugs. 5. Scatchard analysis of the interactions showed that displacement of bilirubin by these drugs occurred principally at the primary, high affinity, low capacity binding site.

show abstract

“…Many studies on the HSA binding properties [2][3][4][5][6][7] have shown that the hydrophobic subdomains IIA and IIIA represent the principal binding regions on HSA.…”

Section: Introductionmentioning

confidence: 99%

Human serum albumin binding ibuprofen: A 3D description of the unfolding pathway in urea

Galantini¹,

Leggio²,

Konarev³

et al. 2010

Biophysical Chemistry

View full text Add to dashboard Cite

This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. A C C E P T E D M A N U S C R I P T ACCEPTED MANUSCRIPT A C C E P T E D M A N U S C R I P T ACCEPTED MANUSCRIPT2 AbstractSmall angle X-ray scattering (SAXS) technique, supported by light scattering measurements and spectroscopic data (circular dichroism and fluorescence) allowed us to restore the 3D structure at low resolution of defatted human serum albumin (HSA) in interaction with ibuprofen. The data were carried out on a set of HSA solutions with urea concentrations between 0.00 and 9.00 M. The SingularValue Decomposition method, applied to the complete SAXS data set allowed us to distinguish three different states in solution. In particular a native conformation N (at 0.00 M urea), an intermediate I1(at 6.05 M urea) and an unfolded structure U (at 9.00 M urea) were recognized. The low resolution structures of these states were obtained by exploiting both ab initio and rigid body fitting methods. In particular, for the protein without denaturant, a conformation recently described (Leggio & al., PCCP, 2008, 10, 6741-6750), very similar to the crystallographic heart shape, with only a slight reciprocal movement of the three domains, was confirmed. The I1 structure was instead characterized by only a closed domain (domain III) and finally, the recovered structure of the U state revealed the characteristic feature of a completely open state. A direct comparison with the free HSA pointed out that the presence of the ibuprofen provokes a shift of the equilibrium towards higher urea concentrations without changing the unfolding sequence. The work represents a type of analysis which could be exploited in future investigations on proteins in solution, in the binding of drugs or endogenous compounds and in the pharmacokinetic properties as well as in the study of allosteric effects, cooperation or anticooperation mechanisms.

show abstract

Specific Binding Sites on Albumin

Cited by 74 publications

References 0 publications

Variations in drug free fraction during alcohol withdrawal.

Variations in drug free fraction during alcohol withdrawal.

The effect of semisynthetic penicillins on the binding of bilirubin by neonatal serum.

Human serum albumin binding ibuprofen: A 3D description of the unfolding pathway in urea

Contact Info

Product

Resources

About