TAILIEUCHUNG - Báo cáo khoa học: Allosteric and binding properties of Asp1–Glu382 truncated recombinant human serum albumin – an optical and NMR spectroscopic investigation

Human serum albumin (HSA) is known for its exceptional ligand-binding capacity; indeed, its modular domain organization provides a variety of ligand-binding sites. Its flexible modular structure involves more than the immediate vicinity of the binding site(s), affecting the ligand-binding prop-erties of the whole protein. | Allosteric and binding properties of Asp1-Glu382 truncated recombinant human serum albumin - an optical and NMR spectroscopic investigation Gabriella Fanali1 Giorgio Pariani1 Paolo Ascenzi2 3 and Mauro Fasano1 1 Dipartimento di Biologia Strutturale e Funzionale Universita dell Insubria Busto Arsizio Italy 2 Istituto Nazionale per le Malattie Infettive IRCCS Lazzaro Spallanzani Roma Italy 3 Laboratorio Interdisciplinare di Microscopia Elettronica Universita Roma Tre Roma Italy Keywords human serum albumin ibuprofen nuclear magnetic relaxation dispersion truncated human serum albumin warfarin Correspondence M. Fasano Dipartimento di Biologia Strutturale e Funzionale University dell Insubria Via A. da Giussano 12 I-21052 Busto Arsizio VA Italy Fax 39 0331 339459 Tel 39 0331 339450 E-mail Received 10 October 2008 revised 29 December 2008 accepted 6 February 2009 doi Human serum albumin HSA is known for its exceptional ligand-binding capacity indeed its modular domain organization provides a variety of ligand-binding sites. Its flexible modular structure involves more than the immediate vicinity of the binding site s affecting the ligand-binding properties of the whole protein. Here biochemical characterization by 1H-NMR relaxometry and optical spectroscopy of a truncated form of HSA tHSA encompassing domains I and II Asp1-Glu382 is reported. Removal of the C-terminal domain III results in a number of contacts that involve domain I containing the heme site and domain II containing the warfarin site being lost however the allosteric linkage between heme and warfarin sites is maintained. tHSA shows a nuclear magnetic relaxation dispersion profile similar to that of HSA and displays increased affinity for ibuprofen warfarin and heme suggesting that the fold is preserved. Moreover the allosteric properties that make HSA a peculiar monomeric protein and account for the regulation of ligand-binding modes by .

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