scholarly journals Intrachain disulfide bond in the core hinge region of human IgG4

1997 ◽  
Vol 6 (2) ◽  
pp. 407-415 ◽  
Author(s):  
James W. Bloom ◽  
Melanie S. Madanat ◽  
David Marriott ◽  
Teresa Wong ◽  
Sham-Yuen Chan
Keyword(s):  
Disulfide Bond ◽  
Hinge Region ◽  
The Core ◽  
Intrachain Disulfide Bond

The Single Disulfide-Directed β-Hairpin Fold: Role of Disulfide Bond in Folding and Effect of an Additional Disulfide Bond on Stability

2020 ◽  
Vol 73 (4) ◽  
pp. 312
Author(s):  
Balasubramanyam Chittoor ◽  
Bankala Krishnarjuna ◽  
Rodrigo A. V. Morales ◽  
Raymond S. Norton
Keyword(s):  
Disulfide Bond ◽  
Disulfide Bonds ◽  
Solution Structure ◽  
Conformational Stability ◽  
Disulfide Bridge ◽  
Solution Nmr ◽  
Peptide Epitope ◽  
The Core ◽  
Native Fold

Disulfide bonds play a key role in the oxidative folding, conformational stability, and functional activity of many peptides. A few disulfide-rich peptides with privileged architecture such as the inhibitor cystine knot motif have garnered attention as templates in drug design. The single disulfide-directed β-hairpin (SDH), a novel fold identified more recently in contryphan-Vc1, has been shown to possess remarkable thermal, conformational, and chemical stability and can accept a short bioactive epitope without compromising the core structure of the peptide. In this study, we demonstrated that the single disulfide bond is critical in maintaining the native fold by replacing both cysteine residues with serine. We also designed an analogue with an additional, non-native disulfide bridge by replacing Gln1 and Tyr9 with Cys. Contryphan-Vc11–22[Q1C, Y9C] was synthesised utilising orthogonal cysteine protection and its solution structure determined using solution NMR spectroscopy. This analogue maintained the overall fold of native contryphan-Vc1. Previous studies had shown that the β-hairpin core of contryphan-Vc1 was resistant to proteolysis by trypsin and α-chymotrypsin but susceptible to cleavage by pepsin. Contryphan-Vc11–22[Q1C, Y9C] proved to be completely resistant to pepsin, thus confirming our design strategy. These results highlight the role of the disulfide bond in maintaining the SDH fold and provide a basis for the design of more stable analogues for peptide epitope grafting.

Synthesis of protected peptides from the human IgG1 hinge region on PEG support using disulfide bond synthons and alkaline or enzymatic detachment

2006 ◽  
Vol 47 (6) ◽  
pp. 1023-1025 ◽  
Author(s):  
Petr Niederhafner ◽  
Martin Šafařík ◽  
Jaroslav Šebestík ◽  
Vladimír Gut ◽  
Petr Maloň ◽  
...  
Keyword(s):  
Disulfide Bond ◽  
Hinge Region ◽  
Human Igg1 ◽  
Protected Peptides

scholarly journals Role of the intrachain disulfide bond of beta2-microglobulin on its amyloid fibril formation.

2001 ◽  
Vol 41 (supplement) ◽  
pp. S169
Author(s):  
Y Ohashi ◽  
Y Hagihara ◽  
Kozhukh Gennadiy ◽  
M Hoshino ◽  
K Hasegawa ◽  
...  
Keyword(s):  
Disulfide Bond ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Amyloid Fibril Formation ◽  
Intrachain Disulfide Bond

scholarly journals Evidence for involvement of IgA1 hinge glycopeptide in the IgA1-IgA1 interaction in IgA nephropathy.

1997 ◽  
Vol 8 (6) ◽  
pp. 915-919 ◽  
Author(s):  
T Kokubo ◽  
Y Hiki ◽  
H Iwase ◽  
A Horii ◽  
A Tanaka ◽  
...  
Keyword(s):  
Sialic Acid ◽  
Iga Nephropathy ◽  
Binding Sites ◽  
Competitive Inhibition ◽  
Hinge Region ◽  
Percent Inhibition ◽  
The Core ◽  
Proline Rich Peptide ◽  
Inhibition Curve

The study was performed to investigate the role of the IgA1 hinge region in the IgA1-IgA1 interaction, which was observed previously in IgA nephropathy. The competitive inhibition assays of the IgA1-IgA1 binding were performed using the following candidates for inhibitors: native IgA1 hinge glycopeptide (nHGP), IgA1, IgA2, and IgG. The IgA1-IgA1 binding was definitely inhibited by the nHGP and the IgA1 (maximum of percent inhibition: 66.1 and 60.5%, respectively). There was no obvious inhibition in the IgA2 and the IgG. The inhibition curves of the nHGP and the IgA1 were significantly different from that of the IgG (P < 0.01, respectively). Furthermore, to reveal the detailed binding sites in the interaction, the same inhibition assays were performed using the following substances composing the IgA1 hinge glycopeptide: galactose (Gal), N-acetyl-galactosamine (GalNAc), Gal beta 1-3GalNAc, sialic acid, tetrapeptide PTPS, and synthesized hinge proline-rich peptide PVPSTPPTPSPSTPPTPSPS (sHP). sHP, Gal beta 1-3GalNAc, Gal, and GalNAc inhibited the binding (69.3, 34.1, 14.9, 14.6%, respectively). No obvious inhibition was observed in sialic acid and tetrapeptide PTPS. The inhibition curve of sHP was significantly different from that of the PTPS (P < 0.05). Those of Gal beta 1-3GalNAc, Gal, and GalNAc were also significantly different from that of sialic acid (P < 0.05, respectively). These results suggested that the IgA1-IgA1 interaction could be mediated by the core structure including the peptide and the sugars, except for sialic acid in the hinge region, resulting in the formation of the circulating macromolecular IgA1 in IgA nephropathy.

The Liptin Haemopoietic Cytokine Fold is Stabilized by an Intrachain Disulfide Bond

1996 ◽  
Vol 28 (12) ◽  
pp. 649-652 ◽  
Author(s):  
F. Rock ◽  
S. Altmann ◽  
M. van Heek ◽  
R. Kastelein ◽  
J. Bazan
Keyword(s):  
Disulfide Bond ◽  
Intrachain Disulfide Bond

Role of the Intrachain Disulfide Bond of Ovalbumin during Conversion into S-Ovalbumin

1996 ◽  
Vol 60 (9) ◽  
pp. 1464-1468 ◽  
Author(s):  
Nobuyuki Takahashi ◽  
Eizo Tatsumi ◽  
Takuya Orita ◽  
Masaaki Hirose
Keyword(s):  
Disulfide Bond ◽  
Intrachain Disulfide Bond
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