Chiral Anionic Coordinated Polymerization of Thiiranes : Enantiomeric Resolution and Disulfide Linkage Formation

1987 ◽  
pp. 297-311 ◽  
Author(s):  
M. Sepulchre ◽  
A. Momtaz ◽  
N. Spassky
Keyword(s):  
Enantiomeric Resolution ◽  
Disulfide Linkage

Enantiomeric resolution of chiral aromatic sulfoxides on non-commercial cellulose tribenzoate plates

2012 ◽  
Vol 25 (3) ◽  
pp. 214-219 ◽  
Author(s):  
Massimo Bubba ◽  
Leonardo Checchini ◽  
Alessandra Cincinelli ◽  
Luciano Lepri
Keyword(s):  
Enantiomeric Resolution

Ratiometric Detection of Glutathione Based on Disulfide Linkage Rupture between a FRET Coumarin Donor and a Rhodamine Acceptor

ChemBioChem ◽  
2021 ◽  
Author(s):  
Yibin Zhang ◽  
Shuai Xia ◽  
Shulin Wan ◽  
Tessa E. Steenwinkel ◽  
Tara Vohs ◽  
...  
Keyword(s):  
Disulfide Linkage ◽  
Ratiometric Detection

scholarly journals Gonococcal pili. Primary structure and receptor binding domain.

1984 ◽  
Vol 159 (5) ◽  
pp. 1351-1370 ◽  
Author(s):  
G K Schoolnik ◽  
R Fernandez ◽  
J Y Tai ◽  
J Rothbard ◽  
E C Gotschlich
Keyword(s):  
Amino Acids ◽  
Receptor Binding ◽  
Binding Domain ◽  
Structural Basis ◽  
Receptor Binding Domain ◽  
Variable Regions ◽  
Disulfide Linkage ◽  
Polymeric Structure ◽  
Antigenic Diversity ◽  
Single Polypeptide Chain

The complete amino acid sequence of pilin from gonococcal strain MS11 and the sequence of constant and variable regions from strain R10 pilin have been determined in order to elucidate the structural basis for adherence function, antigenic diversity, and polymeric structure. The MS11 pilin sequence consists of 159 amino acids in a single polypeptide chain with two cysteines in disulfide linkage and serine-bonded phosphate residues. TC-2 (31-111), a soluble monomeric pilus peptide prepared by arginine-specific digestion, bound human endocervical, but not buccal or HeLa cells and therefore is postulated to encompass the receptor binding domain. Variable regions of CNBr-3 appear to confer antigenic diversity and comprise segments in which changes in the position of charged residues occur in hydrophilic, beta-turns. Residues 2-21 and 202-221 of gonococcal pilins and lower eucaryotic actins, respectively, exhibit 50% homology. When these residues are arranged at intervals of 100 degrees of arc on "helical wheels," the identical amino acids comprise a hydrophobic face on one side of the helix. This observation, the hydrophobic character of this region and the tendency for TC-1 (residues 1-30) to aggregate in water, suggest that this stretch interacts with other subunits to stabilize polymeric structure.

Assigning Peptide Disulfide Linkage Pattern Among Regio-Isomers via Methoxy Addition to Disulfide and Tandem Mass Spectrometry

2017 ◽  
Vol 28 (6) ◽  
pp. 1099-1108 ◽  
Author(s):  
Kirt L. Durand ◽  
Lei Tan ◽  
Craig A. Stinson ◽  
Chasity B. Love-Nkansah ◽  
Xiaoxiao Ma ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Tandem Mass Spectrometry ◽  
Tandem Mass ◽  
Disulfide Linkage ◽  
Linkage Pattern

Application of modified cyclodextrins in capillary electrophoresis for enantiomeric resolution of propranolol and analogues

1995 ◽  
Vol 705 (2) ◽  
pp. 351-361 ◽  
Author(s):  
M.W. Matchett ◽  
S.K. Branch ◽  
T.M. Jefferies
Keyword(s):  
Capillary Electrophoresis ◽  
Enantiomeric Resolution ◽  
Modified Cyclodextrins

Sulfhydryl-selective fluorescence labeling of lipoprotein(a) reveals evidence for one single disulfide linkage between apoproteins(a) and B-100

Biochemistry ◽  
1991 ◽  
Vol 30 (47) ◽  
pp. 11245-11249 ◽  
Author(s):  
Andreas Sommer ◽  
Roland Gorges ◽  
Gerhard M. Kostner ◽  
Fritz Paltauf ◽  
Albin Hermetter
Keyword(s):  
Fluorescence Labeling ◽  
Disulfide Linkage ◽  
Lipoprotein A

Synthesis and Enantiomeric Resolution of Medetomidine

2015 ◽  
Vol 47 (2) ◽  
pp. 141-148 ◽  
Author(s):  
H. Fakhraian ◽  
H. Toulabi ◽  
E. Choobdari ◽  
M. H. Peyrovi ◽  
H. Hadj Ghanbary
Keyword(s):  
Enantiomeric Resolution

Human platelets contain forms of factor V in disulfide-linkage with multimerin

2004 ◽  
Vol 92 (12) ◽  
pp. 1349-1357 ◽  
Author(s):  
Nola Fuller ◽  
Shilun Zheng ◽  
Frédéric Adam ◽  
Samira Jeimy ◽  
Ian Horsewood ◽  
...  
Keyword(s):  
Disulfide Bonds ◽  
Human Platelets ◽  
Factor V ◽  
Single Chain ◽  
Platelet Factor ◽  
Disulfide Linkage ◽  
Factor Va ◽  
Plasma Factor ◽  
Large Platelet ◽  
Large Factor

SummaryFactor V is an essential cofactor for blood coagulation that circulates in platelets and plasma. Unlike plasma factor V, platelet factorV is stored complexed with the polymeric α-granule protein multimerin. In analyses of human platelet factor V on nonreduced denaturing multimer gels, we identified that approximately 25% was variable in size and migrated larger than single chain factor V, the largest form in plasma. Upon reduction, the unusually large, variably-sized forms of platelet factor V liberated components that comigrated with other forms of platelet factor V, indicating that they contained factor V in interchain disulfide-linkages. With thrombin cleavage, factor Va heavy and light chain domains, but not B-domains, were liberated from the components linked by interchain disulfide bonds, indicating that the single cysteine in the B-domain at position 1085 was the site of disulfide linkage. Since unusually large factor V had a variable size and included forms larger than factor V dimers, the data suggested disulfide-linkage with another platelet protein, possibly multimerin. Immunoprecipitation experiments confirmed that unusually large factor V was associated with multimerin and it remained associated in 0.5 M salt. Moreover, platelets contained a subpopulation of multimerin polymers that resisted dissociation from factor V by denaturing detergent and comigrated with unusually large platelet factor V, before and after thrombin cleavage.The disulfide-linked complexes of multimerin and factor V in platelets, which are cleaved by thrombin to liberate factor Va, could be important for modulating the function of platelet factor V and its delivery onto activated platelets. Factor Va generation and function from unusually large platelet factor V is only speculative at this time.

scholarly journals Blastomyces Virulence Adhesin-1 Protein Binding to Glycosaminoglycans Is Enhanced by Protein Disulfide Isomerase

mBio ◽  
2015 ◽  
Vol 6 (5) ◽  
Author(s):  
Audrey Beaussart ◽  
Tristan Brandhorst ◽  
Yves F. Dufrêne ◽  
Bruce S. Klein
Keyword(s):  
Protein Disulfide Isomerase ◽  
Tandem Repeats ◽  
Pathogenic Fungi ◽  
Heparin Binding ◽  
Binding Studies ◽  
Disulfide Linkage ◽  
Disulfide Isomerase ◽  
Atomic Force ◽  
Protein Disulfide

ABSTRACT Blastomyces adhesin-1 (BAD-1) protein mediates the virulence of the yeast Blastomyces dermatitidis, in part by binding host lung tissue, the extracellular matrix, and cellular receptors via glycosaminoglycans (GAGs), such as heparan sulfate. The tandem repeats that make up over 90% of BAD-1 appear in their native state to be tightly folded into an inactive conformation, but recent work has shown that they become activated and adhesive upon reduction of a disulfide linkage. Here, atomic force microscopy (AFM) of a single BAD-1 molecule interacting with immobilized heparin revealed that binding is enhanced upon treatment with protein disulfide isomerase and dithiothreitol (PDI/DTT). PDI/DTT treatment of BAD-1 induced a plateau effect in atomic force signatures that was consistent with sequential rupture of tandem binding domains. Inhibition of PDI in murine macrophages blunted BAD-1 binding to heparin in vitro. Based on AFM, we found that a short Cardin-Weintraub sequence paired with a WxxWxxW sequence in the first, degenerate repeat at the N terminus of BAD-1 was sufficient to initiate heparin binding. Removal of half of the 41 BAD-1 tandem repeats led to weaker adhesion, illustrating their role in enhanced binding. Mass spectroscopy of the tandem repeat revealed that the PDI-induced interaction with heparin is characterized by ruptured disulfide bonds and that cysteine thiols remain reduced. Further binding studies showed direct involvement of thiols in heparin ligation. Thus, we propose that the N-terminal domain of BAD-1 governs the initial association with host GAGs and that proximity to GAG-associated host PDI catalyzes activation of additional binding motifs conserved within the tandem repeats, leading to enhanced avidity and availability of reduced thiols. IMPORTANCE Pathogenic fungi and other microbes must adhere to host tissue to initiate infection. Surface adhesins promote this event and may be required for disease pathogenesis. We studied a fungal adhesin essential for virulence (BAD-1; Blastomyces adhesin-1) and found that host products induce its structural reconfiguration and foster its optimal binding to tissue structures.

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