The Increased Flexibility of CDR Loops Generated in Antibodies by Congo Red Complexation Favors Antigen Binding

Król, Marcin; Roterman, Irena; Drozd, Anna; Konieczny, Leszek; Piekarska, Barbara; Rybarska, Janina; Spólnik, Paweł; Stopa, Barbara

doi:10.1080/07391102.2006.10531235

Cited by 11 publications

(17 citation statements)

References 44 publications

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“…The N-terminal fragment of the light chain V domain has been identified as highly unstable on the basis of experimental results [21]. This conclusion is supported by molecular dynamics simulations involving B-J proteins.…”

Section: Role Of the N-terminal Fragment In V Domainssupporting

confidence: 67%

“…The N-terminal section in the BJ dimer occupies an exposed position, facing the environment. This renders it susceptible to structural changes -it may become uncoiled, freeing itself from the influence of the protein (in the sense of the FOD model) [21]. Figure 5.6 depicts this situation distinguishing the N-terminal fragment and fragments engaged in interface generation as the region of lower stability due to lover engagement in hydrophobic core generation.…”

Section: Role Of the N-terminal Fragment In V Domainsmentioning

confidence: 99%

“…The fuzzy oil drop model reveals the status of the complete protein (complex), its individual domains as well as fragments of polypeptide chains -the presented analysis covers the status of the interface area and the N-terminal fragment which has been experimentally characterized as highly unstable [21]. Table 5.2 presents a comparison of RD parameters describing full-chain dimers and V/C domains present in the complex.…”

Section: Structure Of Hydrophobic Core In B-j Proteinsmentioning

confidence: 99%

“…Under these conditions the target protein usually retains its monocentrichydrophobic core, along with any local deviations associated with natural ligand binding capabilities [28]. The supramolecular ligand may occupy the space vacated by a displaced loop, as indeed observed in the case of IgG V domain [21]. The potential ligand binding site can be recognized using FOD calculation as local hydrophobicity deficiency [28].…”

Section: Complexation Of Congo Redmentioning

confidence: 99%

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Possible Mechanism of Amyloidogenesis of V Domains

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Self-Assembled Molecules – New Kind of Protein Ligands

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This chapter discusses complexation of Congo red by amyloid structures comprising immunoglobulin light chains, particularly the so-called Bence-Jones (BJ) proteins. According to the presented study, in BJ proteins the V domain is substantially less stable than the C domain. This conclusion is based on quantitative analysis of the protein's hydrophobic core, made possible by the fuzzy oil drop model. Results indicate that the V domain exhibits structural ordering characteristic of amyloid aggregates, i.e. linear propagation of local hydrophobicity peaks and troughs rather than a monocentric hydrophobic core (typically present in globular proteins). On this basis, the authors propose a hypothetical arrangement of V domains which leads to formation of an amyloid. Structural similarities between V domains in BJ proteins and other types of amyloid aggregates enable the authors to study the specific mechanism of Congo red complexation by amyloids.The proposed Congo red complexation mechanism builds upon the authors' previous experience with bioinformatics tools. The subject should be of interest to researchers specializing in protein folding studies and misfolding diseases.

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Section: Role Of the N-terminal Fragment In V Domainssupporting

confidence: 67%

Section: Role Of the N-terminal Fragment In V Domainsmentioning

confidence: 99%

Section: Structure Of Hydrophobic Core In B-j Proteinsmentioning

confidence: 99%

Section: Complexation Of Congo Redmentioning

confidence: 99%

See 2 more Smart Citations

Possible Mechanism of Amyloidogenesis of V Domains

Banach

Kalinowska

Konieczny

et al. 2017

Self-Assembled Molecules – New Kind of Protein Ligands

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“…On the other hand, the same phenomenon would tend to inhibit the action of enzymes where the ligand must be released following catalysis. Indeed, such inhibition has been confirmed in the scope of complement activation which depends on the action of convertases [33].…”

Section: Evidences Of Intramolecular Signaling Supplied By Using Congmentioning

confidence: 92%

Supramolecular Congo Red as Specific Ligand of Antibodies Engaged in Immune Complex

Jagusiak

Rybarska

Piekarska

et al. 2017

Self-Assembled Molecules – New Kind of Protein Ligands

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Supramolecular Congo red has been used to validate long-lasting theories regarding intramolecular signaling in antibodies and its relation to activation of the complement system. Strong enhancement of antigen-antibody complexation resulting from the binding of supramolecular ligands enables also polyclonal antibodies having intermediate affinity to trigger complement cascade apart of high affinity antibody fraction. This would not have been possible in the absence of Congo red. The property of antibodies provides specifically their ability to trigger the complement system allowed when sufficient structural strain is produced by antigen complexation provides an evidence of intramolecular signaling.The selective complexation of supramolecular ligands with antibodies engaged in immune complexes enables their using as carriers of drugs in immunotargeting system. Self-associating organic molecules which form ribbonlike micellar structures may, owing to their structural characteristics, penetrate inside proteins and form stable complexes. Such penetration is possible in areas of the protein which have been destabilized, either temporarily or permanently -such as antibody/antigen complexes. Since Congo red (CR) has been used in research as the most typical Keywords

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The use of supramolecular structures as protein ligands

et al. 2013

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Congo red dye as well as other eagerly self-assembling organic molecules which form rod-like or ribbon-like supramolecular structures in water solutions, appears to represent a new class of protein ligands with possible wide-ranging medical applications. Such molecules associate with proteins as integral clusters and preferentially penetrate into areas of low molecular stability. Abnormal, partly unfolded proteins are the main binding target for such ligands, while well packed molecules are generally inaccessible. Of particular interest is the observation that local susceptibility for binding supramolecular ligands may be promoted in some proteins as a consequence of function-derived structural changes, and that such complexation may alter the activity profile of target proteins. Examples are presented in this paper.

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The Increased Flexibility of CDR Loops Generated in Antibodies by Congo Red Complexation Favors Antigen Binding

Cited by 11 publications

References 44 publications

Possible Mechanism of Amyloidogenesis of V Domains

Possible Mechanism of Amyloidogenesis of V Domains

Supramolecular Congo Red as Specific Ligand of Antibodies Engaged in Immune Complex

The use of supramolecular structures as protein ligands

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