Conformational changes involved in thermal aggregation processes of bovine serum albumin

2003 ◽  
Vol 105 (1) ◽  
pp. 133-141 ◽  
Author(s):  
Valeria Militello ◽  
Valeria Vetri ◽  
Maurizio Leone
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Conformational Changes ◽  
Bovine Serum ◽  
Thermal Aggregation ◽  
Aggregation Processes

Influence of metal ions on thermal aggregation of bovine serum albumin: Aggregation kinetics and structural changes

2009 ◽  
Vol 103 (12) ◽  
pp. 1729-1738 ◽  
Author(s):  
Giovanna Navarra ◽  
Anna Tinti ◽  
Maurizio Leone ◽  
Valeria Militello ◽  
Armida Torreggiani
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Metal Ions ◽  
Bovine Serum ◽  
Structural Changes ◽  
Aggregation Kinetics ◽  
Thermal Aggregation

scholarly journals Studies on Thermal Aggregation of Bovine Serum Albumin as a Drug Carrier.

2000 ◽  
Vol 48 (4) ◽  
pp. 464-466 ◽  
Author(s):  
Chikako HONDA ◽  
Hiroko KAMIZONO ◽  
Tomomi SAMEJIMA ◽  
Kazutoyo ENDO
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Drug Carrier ◽  
Thermal Aggregation

scholarly journals Thermally induced conformational changes and protein–protein interactions of bovine serum albumin in aqueous solution under different pH and ionic strengths as revealed by SAXS measurements

2017 ◽  
Vol 19 (26) ◽  
pp. 17143-17155 ◽  
Author(s):  
Dmitry Molodenskiy ◽  
Evgeny Shirshin ◽  
Tatiana Tikhonova ◽  
Andrey Gruzinov ◽  
Georgy Peters ◽  
...  
Keyword(s):  
Aqueous Solution ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Conformational Changes ◽  
Interaction Potential ◽  
Protein Interactions ◽  
Bovine Serum ◽  
Protein Protein Interactions ◽  
Thermally Induced ◽  
Before And After

Temperature-induced oligomerization of albumin before and after protein melting was studied using SAXS and interpreted in terms of interaction potential.

scholarly journals The Importance of Protein-Protein Interactions on the pH-Induced Conformational Changes of Bovine Serum Albumin: A Small Angle X-Ray Scattering Study

2010 ◽  
Vol 98 (3) ◽  
pp. 630a ◽  
Author(s):  
Leandro R.S. Barbosa ◽  
Maria Grazia Ortore ◽  
Francesco Spinozzi ◽  
Paolo Mariani ◽  
Sigrid Bernstorff ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Conformational Changes ◽  
Protein Interactions ◽  
Small Angle ◽  
Bovine Serum ◽  
Protein Protein Interactions ◽  
X Ray ◽  
X Ray Scattering ◽  
Scattering Study

scholarly journals Identifying Reducing and Capping Sites of Protein-Encapsulated Gold Nanoclusters

Molecules ◽  
2019 ◽  
Vol 24 (8) ◽  
pp. 1630 ◽  
Author(s):  
Yu-Chen Hsu ◽  
Mei-Jou Hung ◽  
Yi-An Chen ◽  
Tsu-Fan Wang ◽  
Ying-Ru Ou ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Conformational Changes ◽  
Local Structure ◽  
Bovine Serum ◽  
Gold Nanoclusters ◽  
Cysteic Acid ◽  
Subsequent Growth ◽  
The Core

The reducing and capping sites along with their local structure impact photo properties of the red bovine serum albumin-capped Au nanocluster (BSA-AuNC), however, they are hard to identify. We developped a workflow and relevant techniques using mass spectrometry (MS) to identify the reducing and capping sites of BSA-AuNCs involved in their formation and fluorescence. Digestion without disulfide cleavages yielded an Au core fraction exhibiting red fluorescence and [AunSm] ion signals and a non-core fraction exhibiting neither of them. The core fraction was identified to mainly be comprised of peptides containing cysteine residues. The fluorescence and [AunSm] signals were quenched by tris(2-carboxyethyl)phosphine, confirming that disulfide groups were required for nanocluster stabilization and fluorescence. By MS sequencing, the disulfide pairs, C75–C91/C90–C101 in domain IA, C315–C360/C359–C368 in domain IIB, and C513–C558/C557–C566 in domain IIIB, were identified to be main capping sites of red AuNCs. Peptides containing oxidized cysteines (sulfinic or cysteic acid) were identified as reducing sites mainly in the non-core fraction, suggesting that disulfide cleavages by oxidization and conformational changes contributed to the subsequent growth of nanoclusters at nearby intact disulfide pairs. This is the first report on precise identification of the reducing and capping sites of BSA-AuNCs.

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