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Title: Induced Long-Range Attractive Potentials of Human Serum Albumin by Ligand Binding

Abstract

Small-angle x-ray scattering and dielectric spectroscopy investigation on the solutions of recombinant human serum albumin and its heme hybrid revealed that heme incorporation induces a specific long-range attractive potential between protein molecules. This is evidenced by the enhanced forward intensity upon heme binding, despite no hindrance to rotatory Brownian motion, unbiased colloid osmotic pressure, and discontiguous nearest-neighbor distance, confirming monodispersity of the proteins. The heme-induced potential may play a trigger role in recognition of the ligand-filled human serum albumins in the circulatory system.

Authors:
 [1];  [2];  [3];  [4]; ;  [3]
  1. Division of Pure and Applied Physics, Faculty of Science and Engineering, Waseda University, 3-4-1 Okubo, Shinjuku-ku, Tokyo 169-8555 (Japan)
  2. (Japan)
  3. Advanced Research Institute for Science and Engineering, Waseda University, 3-4-1 Okubo, Shinjuku-ku, Tokyo 169-8555 (Japan)
  4. (JST), 4-1-8 Honcho, Kawaguchi-shi, Saitama 332-0012 (Japan)
Publication Date:
OSTI Identifier:
20951382
Resource Type:
Journal Article
Resource Relation:
Journal Name: Physical Review Letters; Journal Volume: 98; Journal Issue: 20; Other Information: DOI: 10.1103/PhysRevLett.98.208101; (c) 2007 The American Physical Society; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
71 CLASSICAL AND QUANTUM MECHANICS, GENERAL PHYSICS; ALBUMINS; BLOOD SERUM; BROWNIAN MOVEMENT; COLLOIDS; HEME; LIGANDS; SMALL ANGLE SCATTERING; SOLUTIONS; SPECTROSCOPY; X-RAY DIFFRACTION

Citation Formats

Sato, Takaaki, Advanced Research Institute for Science and Engineering, Waseda University, 3-4-1 Okubo, Shinjuku-ku, Tokyo 169-8555, Komatsu, Teruyuki, PRESTO, Japan Science and Technology Agency, Nakagawa, Akito, and Tsuchida, Eishun. Induced Long-Range Attractive Potentials of Human Serum Albumin by Ligand Binding. United States: N. p., 2007. Web. doi:10.1103/PHYSREVLETT.98.208101.
Sato, Takaaki, Advanced Research Institute for Science and Engineering, Waseda University, 3-4-1 Okubo, Shinjuku-ku, Tokyo 169-8555, Komatsu, Teruyuki, PRESTO, Japan Science and Technology Agency, Nakagawa, Akito, & Tsuchida, Eishun. Induced Long-Range Attractive Potentials of Human Serum Albumin by Ligand Binding. United States. doi:10.1103/PHYSREVLETT.98.208101.
Sato, Takaaki, Advanced Research Institute for Science and Engineering, Waseda University, 3-4-1 Okubo, Shinjuku-ku, Tokyo 169-8555, Komatsu, Teruyuki, PRESTO, Japan Science and Technology Agency, Nakagawa, Akito, and Tsuchida, Eishun. Fri . "Induced Long-Range Attractive Potentials of Human Serum Albumin by Ligand Binding". United States. doi:10.1103/PHYSREVLETT.98.208101.
@article{osti_20951382,
title = {Induced Long-Range Attractive Potentials of Human Serum Albumin by Ligand Binding},
author = {Sato, Takaaki and Advanced Research Institute for Science and Engineering, Waseda University, 3-4-1 Okubo, Shinjuku-ku, Tokyo 169-8555 and Komatsu, Teruyuki and PRESTO, Japan Science and Technology Agency and Nakagawa, Akito and Tsuchida, Eishun},
abstractNote = {Small-angle x-ray scattering and dielectric spectroscopy investigation on the solutions of recombinant human serum albumin and its heme hybrid revealed that heme incorporation induces a specific long-range attractive potential between protein molecules. This is evidenced by the enhanced forward intensity upon heme binding, despite no hindrance to rotatory Brownian motion, unbiased colloid osmotic pressure, and discontiguous nearest-neighbor distance, confirming monodispersity of the proteins. The heme-induced potential may play a trigger role in recognition of the ligand-filled human serum albumins in the circulatory system.},
doi = {10.1103/PHYSREVLETT.98.208101},
journal = {Physical Review Letters},
number = 20,
volume = 98,
place = {United States},
year = {Fri May 18 00:00:00 EDT 2007},
month = {Fri May 18 00:00:00 EDT 2007}
}