Where are the disulfide bonds in antibodies?

A typical IgG1 antibody contains two identical light chains and two identical heavy chains. It contains a total of 16 disulfide bonds including 4 inter chain disulfide bonds in the hinge region and 12 intra chain disulfide bonds associated with 12 individual domains (Figure 1).

Does thiol form disulfide bonds?

Disulfide bonds in proteins are formed between the thiol groups of cysteine residues by the process of oxidative folding. The other sulfur-containing amino acid, methionine, cannot form disulfide bonds.

How many disulfide bonds are in growth hormone?

Growth hormone (GH) structure is stabilised by two disulphide bonds, C53-C165 and C182-C189 in human GH.

How many bonds are in a disulfide?

The redox stability of disulfide bonds in proteins can vary over an enormous range. Proteins with the thioredoxin fold have active sites comprising a shared Cys1-Xaa2-Yaa3-Cys4 motif, in which the two cysteines are reversibly disulfide bonded.

How does disulfide bond reduction affect antibody manufacturing?

Antibody disulfide bond reduction has been a challenging issue in monoclonal antibody manufacturing. It could lead to decrease of product purity and failure to meet targeted product profile and/or specifications. More importantly, disulfide bond reduction could also impact drug safety and efficacy.

What are the disulfide bond structures of IgG molecules?

DOI: 10.4161/mabs.4.1.18347 Abstract The disulfide bond structures established decades ago for immunoglobulins have been challenged by findings from extensive characterization of recombinant and human monoclonal IgG antibodies.

Are there any free sulfhydryls in IgG antibodies?

Although, cysteine residues should be in the disulfide bonded states, free sulfhydryls have been detected in all subclasses of IgG antibodies. In addition, disulfide bonds are susceptible to chemical modifications, which can further generate structural variants such as IgG antibodies with trisulfide bond or thioether linkages.

How are disulfide bonds used to stabilize proteins?

A pair of cysteines in close proximity will oxidatively react to form a disulfide bond that fixes and stabilizes the tertiary structure of a protein. Immunoglobulin G (IgG) includes several disulfide bonds, and the patterns of inter-chain disulfide bonds characterize different IgG sub-classes.