Label-free fluorescence turn-on strategy for trypsin activity based on thiolate-protected gold nanoclusters with bovine serum albumin as the substrate

2017 ◽  
Vol 247 ◽  
pp. 392-399 ◽  
Author(s):  
Dan Zhao ◽  
Chuanxia Chen ◽  
Jiahui Zhao ◽  
Jian Sun ◽  
Xiurong Yang
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Gold Nanoclusters ◽  
Label Free ◽  
Trypsin Activity ◽  
Turn On ◽  
Fluorescence Turn On

A fluorescence turn-on probe for human (bovine) serum albumin based on the hydrolysis of a dioxaborine group promoted by proteins

2017 ◽  
Vol 53 (48) ◽  
pp. 6432-6435 ◽  
Author(s):  
Qian Sun ◽  
Weisi Wang ◽  
Zhaoyang Chen ◽  
Yuhua Yao ◽  
Weibing Zhang ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
High Selectivity ◽  
Biologically Relevant ◽  
Turn On ◽  
Fluorescence Turn On ◽  
Hydrolysis Of

A reaction-based florescence probe CBF for serum albumin (SA) was proposed by connecting a dioxaborine unit with environment-sensitive coumarin fluorophore. CBF exhibits high selectivity and sensitivity toward SA over other biologically relevant species and has potential of detecting SA in biosamples.

Digestive processes of haematophagous insects. XII. Secretion of trypsin and carboxypeptidase B by Glossina morsitans morsitans Westwood (Diptera: Glossinidae)

1977 ◽  
Vol 55 (1) ◽  
pp. 215-222 ◽  
Author(s):  
R. H. Gooding
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Protein Content ◽  
Bovine Serum ◽  
Significant Positive Correlation ◽  
Glossina Morsitans Morsitans ◽  
Trypsin Activity ◽  
Glossina Morsitans ◽  
Carboxypeptidase B ◽  
Positive Correlation

There was a significant positive correlation between protein content and the amounts of trypsin and carboxypeptidase B (CPB) in the digestive portion of the midgut of Glossina morsitans morsitans, 24, 48, 72, and 96 h after feeding on a rabbit. CPB and trypsin activity were also positively correlated. Trypsin and CPB production were stimulated, to varying degrees, by bovine serum albumin (BSA), α-globulin, β-globulin, γ-globulin, and haemoglobin; the greatest response was to BSA. Peptides derived from BSA by trypsin cleavage also stimulated production of trypsin and CPB.

Deciphering the positional impact of chlorine in a new series of berberine analogues towards the superb-selective “turn-on” hydrophobic signaling of bovine serum albumin at physiological pH

2020 ◽  
Vol 44 (5) ◽  
pp. 1761-1771 ◽  
Author(s):  
Gopal Chandra Jana ◽  
Sk Nayim ◽  
Nandan Kumar Sahoo ◽  
Somnath Das ◽  
Mt Nasima Aktara ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Limit Of Detection ◽  
Selective Detection ◽  
Turn On

We report a new 9-O-benzyl substituted berberine analogue for the selective detection of BSA with a limit of detection value of 3.30 nM.

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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