scholarly journals Conformational stability and warfarin-binding properties of human serum albumin studied by recombinant mutants

2001 ◽  
Vol 357 (1) ◽  
pp. 269 ◽  
Author(s):  
Hiroshi WATANABE ◽  
Ulrich KRAGH-HANSEN ◽  
Sumio TANASE ◽  
Keisuke NAKAJOU ◽  
Maki MITARAI ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Conformational Stability ◽  
Binding Properties

Conformational stability and warfarin-binding properties of human serum albumin studied by recombinant mutants

2001 ◽  
Vol 357 (1) ◽  
pp. 269-274 ◽  
Author(s):  
Hiroshi WATANABE ◽  
Ulrich KRAGH-HANSEN ◽  
Sumio TANASE ◽  
Keisuke NAKAJOU ◽  
Maki MITARAI ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Expression System ◽  
Conformational Stability ◽  
Affinity Binding ◽  
Binding Properties ◽  
High Affinity Binding ◽  
Yeast Expression System ◽  
High Affinity

Correctly folded recombinant wild-type human serum albumin and the single-residue mutants K199A, W214A, R218H and H242Q were produced with the use of a yeast expression system. The changes in R218H resulted in a pronounced decrease in intrinsic fluorescence. Thermodynamic parameters for thermal denaturation of the present mutants and of five additional mutants have been determined, showing small increases in stability for two mutants (R218H and H242Q) and a larger decrease in stability for one (W214A). In the last of these, denaturation was a heterogeneous process starting at physiological temperature. The high-affinity binding constant for warfarin at pH7.4 was determined by fluorescence spectroscopy: there was a significant increase in affinity for binding of warfarin to H242Q and K199A and a smaller decrease in affinity for W214A and R218H. The findings show that Trp-214 is not as essential for the high-affinity binding of warfarin as has previously been thought.

scholarly journals Conformational stability as a quality attribute for the cell therapy raw material human serum albumin

RSC Advances ◽  
2021 ◽  
Vol 11 (25) ◽  
pp. 15332-15339
Author(s):  
Evelien Wynendaele ◽  
Gamaliel Junren Ma ◽  
Xiaolong Xu ◽  
Nam-Joon Cho ◽  
Bart De Spiegeleer
Keyword(s):  
Human Serum Albumin ◽  
Cell Therapy ◽  
Serum Albumin ◽  
Human Serum ◽  
Conformational Stability ◽  
Raw Material ◽  
Quality Attribute ◽  
Global Measure ◽  
Pharmaceutical Quality

An overall attribute for the consistency in pharmaceutical quality of human serum albumin encompasses a global measure of conformational stability, as measured by CD, DLS, QCM-D or LSPR.

Cigarette smoke induces alterations in the drug-binding properties of human serum albumin

2014 ◽  
Vol 52 (4) ◽  
pp. 166-174 ◽  
Author(s):  
Marco Clerici ◽  
Graziano Colombo ◽  
Francesco Secundo ◽  
Nicoletta Gagliano ◽  
Roberto Colombo ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Cigarette Smoke ◽  
Drug Binding ◽  
Binding Properties

scholarly journals Combined spectroscopy methods and molecular simulations for the binding properties of trametinib to human serum albumin

RSC Advances ◽  
2018 ◽  
Vol 8 (9) ◽  
pp. 4742-4749 ◽  
Author(s):  
Zili Suo ◽  
Qiaomei Sun ◽  
Hongqin Yang ◽  
Peixiao Tang ◽  
Ruixue Gan ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Molecular Simulations ◽  
Binding Properties

Probing the binding properties of trametinib to human serum albumin.

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