pegylation is a well-established technique utilized to overcome the problems related to the therapeutic applications of peptides and proteins. reasons for the pegylation of these biological macromolecules include reducing immunogenicity, proteolytic degradation and rapid clearance from blood circulation. octreotide is an octapeptide analogue of naturally-occurred somatostatin. this peptide has ...

The zinc(II) complex [Zn2(dmdtc)2(μ-dmdtc)2] has been synthesized directly from thiram ligand, containing a disulfide bond {dmdtc = N,N-dimethyldithiocarbamate; thiram = N,N-tetramethylthiuram disulfide}, and characterized by elemental analysis and spectroscopic methods. Surprisingly thiram, undergoes a reductive disulfide bond scission upon reaction with Zn2+ in methanolic media to give the [Z...

the zinc(ii) complex [zn2(dmdtc)2(μ-dmdtc)2] has been synthesized directly from thiram ligand, containing a disulfide bond {dmdtc = n,n-dimethyldithiocarbamate; thiram = n,n-tetramethylthiuram disulfide}, and characterized by elemental analysis and spectroscopic methods. surprisingly thiram, undergoes a reductive disulfide bond scission upon reaction with zn2+ in methanolic media to give the [z...

the zinc(ii) complex [zn2(dmdtc)2(μ-dmdtc)2] has been synthesized directly from thiram ligand, containing a disulfide bond {dmdtc = n,n-dimethyldithiocarbamate; thiram = n,n-tetramethylthiuram disulfide}, and characterized by elemental analysis and spectroscopic methods. surprisingly thiram, undergoes a reductive disulfide bond scission upon reaction with zn2+ in methanolic media to give the [z...

Protein disulfide isomerases (PDIs), a family of thiol-disulfide oxidoreductases that are ubiquitous in all eukaryotes, are the principal catalysts for disulfide bond formation. Here, we investigated three rice (Oryza sativa) PDI family members (PDIL1;1, PDIL1;4, and PDIL2;3) and found that PDIL1;1 exhibited the highest catalytic activity for both disulfide bond formation and disulfide bond red...

objective(s): carbon nanotube (cnt) has been widely applied at molecular and cellular levels due to its exceptional properties. studies based on conjugation of cnts with biological molecules indicated that biological activity is preserved. polyethylenimine (pei) is explored in designing novel gene delivery vectors due to its ability to condense plasmid dna through electrostatic attraction. in t...

MOTIVATION Prediction of disulfide bond connectivity facilitates structural and functional annotation of proteins. Previous studies suggest that cysteines of a disulfide bond mutate in a correlated manner. RESULTS We developed a method that analyzes correlated mutation patterns in multiple sequence alignments in order to predict disulfide bond connectivity. Proteins with known experimental st...

Protein disulfide bond formation contributes to the folding and activity of many exported proteins in bacteria. However, information about disulfide bond formation is limited to only a few bacterial species. We used a multifaceted bioinformatic approach to assess the capacity for disulfide bond formation across this biologically diverse group of organisms. We combined data from a cysteine count...

Background: Some resources have suggested that genetically inactivated pertussis toxoid (PTs) bear a more protective effect than chemically inactivated products. This study aimed to produce new version of PT, by cloning an inactive pertussis toxin S1 subunit (PTS1) in a fusion form with N-terminal half of the listeriolysin O (LLO) pore-forming toxin. Methods: Deposited pdb structure file of the...

A functional disulfide bond in both the HIV envelope glycoprotein, gp120, and its immune cell receptor, CD4, is involved in viral entry, and compounds that block cleavage of the disulfide bond in these proteins inhibit HIV entry and infection. The disulfide bonds in both proteins are cleaved at the cell surface by the small redox protein, thioredoxin. The target gp120 disulfide and its mechanis...