Bovine serum albumin as a universal suppressor of non-specific peptide binding in vials prior to nano-chromatography coupled mass-spectrometry analysis

2015 ◽  
Vol 893 ◽  
pp. 57-64 ◽  
Author(s):  
Sergey I. Kovalchuk ◽  
Nikolay A. Anikanov ◽  
Olga M. Ivanova ◽  
Rustam H. Ziganshin ◽  
Vadim M. Govorun
Keyword(s):  
Mass Spectrometry ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Peptide Binding ◽  
Mass Spectrometry Analysis ◽  
Spectrometry Analysis ◽  
Specific Peptide

Corona protein impacts on alternating current biosusceptometry signal and circulation times of differently coated MnFe2O4 nanoparticles

Nanomedicine ◽  
2021 ◽  
Author(s):  
Andre Gonçalves Prospero ◽  
Lais Pereira Buranello ◽  
Carlos AH Fernandes ◽  
Lucilene Delazari dos Santos ◽  
Guilherme Soares ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Signal Intensity ◽  
Alternating Current ◽  
Circulation Time ◽  
Mass Spectrometry Analysis ◽  
Spectrometry Analysis

Background: We evaluated the impacts of corona protein (CP) formation on the alternating current biosusceptometry (ACB) signal intensity and in vivo circulation times of three differently coated magnetic nanoparticles (MNP): bare, citrate-coated and bovine serum albumin-coated MNPs. Methods: We employed the ACB system, gel electrophoresis and mass spectrometry analysis. Results: Higher CP formation led to a greater reduction in the in vitro ACB signal intensity and circulation time. We found fewer proteins forming the CP for the bovine serum albumin-coated MNPs, which presented the highest circulation time in vivo among the MNPs studied. Conclusion: These data showed better biocompatibility, stability and magnetic signal uniformity in biological media for bovine serum albumin-coated MNPs than for citrate-coated MNPs and bare MNPs.

Interaction of Bovine Serum Albumin and Lysozyme with Stainless Steel Studied by Time-of-Flight Secondary Ion Mass Spectrometry and X-ray Photoelectron Spectroscopy

Langmuir ◽  
2012 ◽  
Vol 28 (47) ◽  
pp. 16306-16317 ◽  
Author(s):  
Yolanda S. Hedberg ◽  
Manuela S. Killian ◽  
Eva Blomberg ◽  
Sannakaisa Virtanen ◽  
Patrik Schmuki ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Stainless Steel ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Photoelectron Spectroscopy ◽  
Bovine Serum ◽  
Secondary Ion Mass Spectrometry ◽  
Time Of Flight ◽  
X Ray ◽  
Secondary Ion

scholarly journals Regulation of Insulin Secretion by SIRT4, a Mitochondrial ADP-ribosyltransferase

2007 ◽  
Vol 282 (46) ◽  
pp. 33583-33592 ◽  
Author(s):  
Nidhi Ahuja ◽  
Bjoern Schwer ◽  
Stefania Carobbio ◽  
David Waltregny ◽  
Brian J. North ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Insulin Secretion ◽  
Amino Acid ◽  
Bovine Serum Albumin ◽  
Matrix Protein ◽  
Mass Spectrometry Analysis ◽  
Carrier Proteins ◽  
Β Cells ◽  
Spectrometry Analysis ◽  
Adp Ribosyltransferase

Sirtuins are homologues of the yeast transcriptional repressor Sir2p and are conserved from bacteria to humans. We report that human SIRT4 is localized to the mitochondria. SIRT4 is a matrix protein and becomes cleaved at amino acid 28 after import into mitochondria. Mass spectrometry analysis of proteins that coimmunoprecipitate with SIRT4 identified insulindegrading enzyme and the ADP/ATP carrier proteins, ANT2 and ANT3. SIRT4 exhibits no histone deacetylase activity but functions as an efficient ADP-ribosyltransferase on histones and bovine serum albumin. SIRT4 is expressed in islets of Langerhans and colocalizes with insulin-expressing β cells. Depletion of SIRT4 from insulin-producing INS-1E cells results in increased insulin secretion in response to glucose. These observations define a new role for mitochondrial SIRT4 in the regulation of insulin secretion.

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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