NMR paper The binding of 5-fluorouracil to native and modified human serum albumin: UV, CD, and

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[NMR paper] The binding of 5-fluorouracil to native and modified human serum albumin: UV, CD, and

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NMR processing:

MDD

NMR assignment:

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Side-chains:

NOEs:

Structure from NMR restraints:

Ab initio:

Fragment-based:

Rosetta-NMR (Robetta)

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GeNMR

I-TASSER

Refinement:

Amber

Structure from chemical shifts:

Fragment-based:

Homology-based:

Torsion angles from chemical shifts:

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TALOS

Promega- Proline

Secondary structure from chemical shifts:

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TALOS

MICS caps, β-turns

d2D

PECAN

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HADDOCK

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08-22-2010, 03:50 AM

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The binding of 5-fluorouracil to native and modified human serum albumin: UV, CD, and

The binding of 5-fluorouracil to native and modified human serum albumin: UV, CD, and 1H and 19F NMR investigation.

Related Articles The binding of 5-fluorouracil to native and modified human serum albumin: UV, CD, and 1H and 19F NMR investigation.

J Pharm Biomed Anal. 1995 Aug;13(9):1087-93

Authors: Bertucci C, Ascoli G, Uccello-Barretta G, Di Bari L, Salvadori P

5-Fluorouracil (FU) is an important and widely used antineoplastic drug that is carried in the serum by plasma proteins. Protein binding studies of this drug to human serum albumin (HSA) have been carried out by several spectroscopic techniques. Difference circular dichroism and UV studies provided information on the class of binding sites involved in the interaction. In particular, displacement experiments showed that FU has at least one secondary binding site in the coumarin binding area, but does not interact with the benzodiazepine binding area. Binding was also investigated by difference 1H NMR and by measuring the increase in the 19F NMR signal of FU when bound to HSA. Finally, evidence was obtained that chemical acetylation of Lys199 results in a decreased apparent binding affinity constant (nK) for FU. Such a modification is induced under physiological conditions by aspirin.

PMID: 8573632 [PubMed - indexed for MEDLINE]

Source: PubMed

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