Human serum albumin-stabilized gold nanoclusters act as an electron transfer bridge supporting specific electrocatalysis of bilirubin useful for biosensing applications

2016 ◽  
Vol 111 ◽  
pp. 7-14 ◽  
Author(s):  
Mallesh Santhosh ◽  
Somasekhar R. Chinnadayyala ◽  
Naveen K. Singh ◽  
Pranab Goswami
Keyword(s):  
Electron Transfer ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Gold Nanoclusters

scholarly journals Human serum albumin encapsulated gold nanoclusters: effects of cluster synthesis on natural protein characteristics

2016 ◽  
Vol 4 (42) ◽  
pp. 6876-6882 ◽  
Author(s):  
B. A. Russell ◽  
B. Jachimska ◽  
I. Kralka ◽  
P. A. Mulheran ◽  
Y. Chen
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Gold Nanoclusters ◽  
Physiochemical Properties ◽  
Natural Protein

The differences in the physiochemical properties between native Human Serum Albumin (HSA) and HSA encapsulated gold nanoclusters (HSA-AuNCs) are characterised.

scholarly journals Probing the Sudlow binding site with warfarin: how does gold nanocluster growth alter human serum albumin?

2016 ◽  
Vol 18 (33) ◽  
pp. 22874-22878 ◽  
Author(s):  
B. A. Russell ◽  
P. A. Mulheran ◽  
D. J. S. Birch ◽  
Y. Chen
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Site ◽  
Gold Nanoclusters ◽  
Drug Binding ◽  
Gold Nanocluster ◽  
Drug Binding Site ◽  
Major Drug

Gold Nanoclusters (AuNCs) synthesised using Human Serum Albumin (HSA) as a stable scaffold are shown to modify the major drug binding site, Sudlow site I. Upon AuNC nucleation within HSA, warfarin was observed to no longer bind to Sudlow I, remaining free in solution.

Photosensitized damage of protein by fluorinated diethoxyphosphorus(V)porphyrin

2013 ◽  
Vol 17 (01n02) ◽  
pp. 56-62 ◽  
Author(s):  
Kazutaka Hirakawa ◽  
Keito Azumi ◽  
Yoshinobu Nishimura ◽  
Tatsuo Arai ◽  
Yoshio Nosaka ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Singlet Oxygen ◽  
Human Serum ◽  
Transfer Mechanism ◽  
Water Soluble ◽  
Electron Transfer Mechanism ◽  
Oxygen Generation ◽  
Singlet Oxygen Generation

The effect of the axial ligand fluorination of the water-soluble P(V)porphyrin complex on photosensitized protein damage was examined. The activity of singlet oxygen generation by diethoxyP(V) porphyrin was slightly improved by the fluorination of the ethoxy chains. Absorption spectrum measurements demonstrated the binding interaction between the P(V)porphyrins and human serum albumin, a water-soluble protein. Photo-irradiated P(V)porphyrins damaged the amino acid residue of human serum albumin, resulting in the decrease of the fluorescence intensity from the tryptophan residue of human serum albumin. A singlet oxygen quencher, sodium azide, could not completely inhibit the damage of human serum albumin, suggesting that the electron transfer mechanism contributes to protein damage as does singlet oxygen generation. The decrease of the fluorescence lifetime of P(V)porphyrin by human serum albumin supported the electron transfer mechanism. The estimated contributions of the electron transfer mechanism are 0.57 and 0.44 for the fluorinated and non-fluorinated P(V)porphyrins, respectively. The total quantum yield of the protein photo-oxidation was slightly enhanced by this axial fluorination.

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