Direct single-step surface plasmon resonance analysis of interactions between small peptides and immobilized monoclonal antibodies

Gomes, Paula; Giralt, Ernest; Andreu, David

doi:10.1016/s0022-1759(99)00218-5

Cited by 23 publications

(22 citation statements)

References 25 publications

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“…As we have shown earlier, despite the fairly small size (ca. 1.6 kDa) of the peptides, reliable data can be obtained with this analysis configuration [10,11]. All the measurable interactions fitted to the pseudo-first-order Table 3 Affinity data for the interactions between mAbs SD6, 4C4 and 3E5, and peptides from the G-H loops of FMDV C-S8c1, C 1 -Brescia and C-S30 mAb Peptide a K A(kin1) , affinity from SPR kinetic analysis with immobilized mAb; K A(kin2) , affinity from SPR kinetic analysis with immobilized peptide; K i(sol.…”

Section: Direct Spr Analysis Of Small Peptidesmentioning

confidence: 85%

Antigenicity modulation upon peptide cyclization: application to the GH loop of foot-and-mouth disease virus strain C1-Barcelona

Gomes

Giralt

Andreu

2001

Vaccine

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Foot-and-mouth disease virus (FMDV) isolate C 1 -Barcelona (or C-S30) includes four replacements within its immunodominant site (GH loop, residues 136-150 of capsid protein VP1, YTTSTRGDLAHVTAT), relative to reference strain C-S8c1 (YTASAR-GDLAHLTTT). Although one of the mutations in C-S30 ( 147 Leu Val) is known to be detrimental for antibody recognition, reactivity of this isolate with the neutralizing monoclonal antibody (mAb) 4C4, raised against FMDV C 1 -Brescia (GH loop: YTASTRGDLAHLTAT), was indistinguishable from those of strains C-S8c1 or C 1 -Brescia. A structural interpretation for these somewhat striking findings is available, based on the observation that 15-residue peptides reproducing the C-S30 and C-S8c1 GH loops adopt very similar, quasi-circular, conformations in crystal complexes with 4C4. Nevertheless, surface plasmon resonance (SPR) kinetic analyses of the interactions between these peptides and three anti-GH loop mAbs have now revealed that the linear C-S30 peptides were less antigenic in solution than their C-S8c1 and C 1 -Brescia counterparts. We have, therefore, tried to modulate peptide antigenicity in solution by cyclization. Functional SPR and structural two dimensional proton nuclear magnetic resonance (2D-1 H NMR) studies of both linear and cyclic peptide antigens are discussed here. Conformation seems to have an important role in peptide antigenicity, even when continuous (i.e. linear) antigenic sites are involved.

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Section: Direct Spr Analysis Of Small Peptidesmentioning

confidence: 85%

Antigenicity modulation upon peptide cyclization: application to the GH loop of foot-and-mouth disease virus strain C1-Barcelona

Gomes

Giralt

Andreu

2001

Vaccine

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“…29 This phenomenon may be caused by the mass transport, steric hindrance, crowding and aggregation of high capacity surface. [30][31][32] Secondly, the COX-2 is high-cost. Figure 4 shows the adsorption curve of the COX-2 (5 µg/mL) on the MPA monolayer for 80 min.…”

Section: Immobilization Of Cox-2mentioning

confidence: 99%

Kinetic Analysis of the Interaction between Nonsteroidal Anti‐inflammatory Drugs and Cyclooxygenase‐2 Using Wavelength Modulation Surface Plasmon Resonance

Liu

Zhao

2011

Chin. J. Chem.

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A surface plasmon resonance (SPR) biosensor based on wavelength modulation technology was developed and validated for the kinetic analysis of the interactions between two nonsteroidal anti-inflammatory drugs (NSAIDs) and cyclooxygenase-2 (COX-2). After the effect of different concentration COX-2 on the binding capacity of the SPR biosensor surface was studied, the COX-2 was immobilized covalently onto the biosensor surface using a standard amine coupling method. The affinity constants for indomethacin, ketoprofen binding to COX-2 are 7.5×10 3 L/mol and 9.25×10 3 L/mol, respectively. The biosensor surface can be regenerated after being rinsed with 0.01 mol/L NaOH, and the biosensor can be used repeatedly. These indicated that the wavelength modulation SPR biosensor has the potential application in the fields of pharmacokinetics, pharmacodynamics and drug discovery.

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“…In our work with foot‐and‐mouth disease virus (FMDV) (11,12), we have encountered examples of a relatively broad recognition of variant peptides by antibodies (10,13–18). These peptides were based on the main antigenic site of FMDV, termed site A, located on the highly flexible GH loop defined by residues 136–150 of the capsid protein VP1 in FMDV isolate C‐S8c1 (19).…”

Section: General Data On the Synthetic Peptides Under Studymentioning

confidence: 99%

Probing degeneracy in antigen–antibody recognition at the immunodominant site of foot‐and‐mouth disease virus

Gomes

Giralt

Ochoa

et al. 2002

The Journal of Peptide Research

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Antigen-antibody binding is regarded as one of the most representative examples of specific molecular recognition in nature. The simplistic view of antigenic recognition in terms of a lock-and-key mechanism is obsolete, as it is evident that both antigens and antibodies are flexible and can undergo substantial mutual adaptation. This flexibility is the source of complexities such as degeneracy and nonadditivity in antigenic recognition. We have used surface plasmon resonance to study the effects of combining multiple amino acid replacements within the sequence of the antigenic GH loop of foot-andmouth disease virus. Our aim was 2-fold: to explore the extent to which antigenic degeneracy can be extended in this particular case, and to search for potential nonadditive effects in introducing multiple amino acid replacements. Combined analysis of one such multiply substituted peptide by SPR, solution NMR and X-ray diffraction shows that antigenic degeneracy can be expected as long as residues directly interacting with the paratope are conserved and the peptide bioactive folding is unaltered. replacements is also remarkable because of its nonconservative character: Phe is much larger than Ala; Pro is a known disrupter of secondary structure, which Ala is not; finally, the Gly 142 R Ser mutation affects the highly conserved RGD motif. Studying the effect that every possible combination of these five mutations has on antigenicity provides a feasible way to explore the relative limits of antigenic degeneracy at this particular site. In addition, previous evidence of positive nonadditivity in multiple substitutions within the GH loop (10,13,16-18) encouraged us to look for possible synergistic effects in the simultaneous combination of these amino acid replacements. Therefore, we analyzed the 31 peptides (Table 1) corresponding to the combination of the five mutations by surface plasmon resonance (SPR) (25,26) against three anti-GH loop mAbs with epitope specificities outlined in Results PeptidesThirty-three 15-residue peptides (Table 1) were synthesized, one representing site A of FMDV C-S8c1 (A15), another as Solution affinity SPR analysisThe viability of direct kinetic biosensor analysis of the interactions between immobilized anti-FMDV mAbs and soluble 15-residue peptides has been previously demonstrated (14,15,17,18,28). In this study, however, most interactions could not be described kinetically, because of high association rates, extremely slow dissociation rates or incomplete surface regeneration (not shown). Deviations from the ideal behavior (29) Table 2 and confirm the high peptideantibody affinities expected in view of the avidity effects observed in the kinetic SPR analyses. These high peptide antigenicities were in agreement with a competition ELISA screening of these peptides using the same anti-GH loop mAbs (Gomes et al., unpublished data) and with the avidity effects observed in the initial kinetic approach.The multiply substituted peptides displayed antigenicities that generally correlat...

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Direct single-step surface plasmon resonance analysis of interactions between small peptides and immobilized monoclonal antibodies

Cited by 23 publications

References 25 publications

Antigenicity modulation upon peptide cyclization: application to the GH loop of foot-and-mouth disease virus strain C1-Barcelona

Antigenicity modulation upon peptide cyclization: application to the GH loop of foot-and-mouth disease virus strain C1-Barcelona

Kinetic Analysis of the Interaction between Nonsteroidal Anti‐inflammatory Drugs and Cyclooxygenase‐2 Using Wavelength Modulation Surface Plasmon Resonance

Probing degeneracy in antigen–antibody recognition at the immunodominant site of foot‐and‐mouth disease virus

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