DOI: 10.1002/jmr.300080405. Kinetic analysis of the interaction between protein a domain variants and human Fc using plasmon resonance detection

Kinetic analysis of the interaction between protein a domain variants and human Fc using plasmon resonance detection

10.1002/jmr.300080405

Crossref journal-article

Wiley

Journal of Molecular Recognition (311)

Abstract

AbstractA real time biospecific interaction analysis (BIA) was performed to study the specific interaction between the Fc portion of human immunoglobulin G1 (Fc1) and a one domain analogue (designated Z) of staphylococcal protein A, in monovalent (Z) and divalent (ZZ) forms, and five different single amino acid substituted Z variants (L17D, N28A, F30A, I31A, K35A). Experimental BIA data were used to calculate association rate constants (Kon), dissociation rate constants (koff). The divalent form (ZZ) showed a higher affinity for Fc1 mainly because of a slower off rate. Out of the five mutant Z protein, four (L17D, N28A, I31A, K35A) four had the major effect to Fc1 compared to the parent Z molecule. Surprisingly, two (L17D, I31A) of these four had the major effect of a decreased binding energy as a lowered kon while the other two (N28A, K35A) mutant proteins showed an increased koff as the major kinetic difference from Z in their binding to Fc1. For five of the six different Z variants, as well as for the ZZ molecule, calculated kaff and calculated differences in binding free energies relative to the parent Z molecule (ΔΔG), are in good agreement with the corresponding values obtained in a competitive displacement assay using radioactively labeled Z as a tracer (Cedergren et al., (1993) Prot. Eng. 6, 441‐448). However, the I31A variant, with a measured kon that was more than three orders of magnitude lower than that of Z in the BIA assay, showed a significant weaker affinity to FcI when calculated from BIA data compared ot the competitive displacement assay. The discrepancy between these two methods for Z(I31A) is discussed as well as possible explanations for the unexpected large effect of lowered kon for two of the mutant Z proteins.

Bibliography

Jendeberg, L., Persson, B., Andersson, R., Karlsson, R., UhlÃ©n, M., & Nilsson, B. (1995). Kinetic analysis of the interaction between protein a domain variants and human Fc using plasmon resonance detection. Journal of Molecular Recognition, 8(4), 270â278. Portico.

Authors 6

Lena Jendeberg (first)
Björn Persson (additional)
Roland Andersson (additional)
Robert Karlsson (additional)
Mathias Uhlén (additional)
Björn Nilsson (additional)

References 30 Referenced 79

10.1021/bi00129a007
10.1021/bi00142a019
10.1006/abio.1993.1484
10.1093/protein/6.4.441
10.1006/jmbi.1993.1611
10.1021/bi00512a001
10.1515/bchm2.1978.359.2.975
Eliasson M.(1990). Streptococcal protein G‐Structure and function. PhD Thesis. Royal Institute of Technology Stockholm.
10.1021/jm00145a002
10.1021/bi00155a020
10.1016/S0006-3495(92)81788-5
10.1016/S0021-9258(20)80776-5 / J. Biol. Chem. / Development of an artificial antibody system with multiple valency using a Fv fragment fused to a fragment of protein A by Ito W. (1993)
10.1016/0022-1759(91)90331-9
10.1107/S0021889891004399
10.1515/zna-1968-1247 / Z. Naturforsch. / Radioactive decay of non radiative surface plamons excited by light by Kretschmann E. (1968)
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10.1016/0161-5890(93)90044-C
10.1021/bi00082a001
10.1039/c39900001526
10.1002/jmr.300070102
{'key': 'e_1_2_1_22_1', 'first-page': '7487', 'article-title': 'Staphylococcal protein A consists of five lgG‐binding domains', 'volume': '14', 'author': 'Moks T.', 'year': '1986', 'journal-title': 'Eur. J. Biochem.'} / Eur. J. Biochem. / Staphylococcal protein A consists of five lgG‐binding domains by Moks T. (1986)
10.1016/0076-6879(90)85015-G
10.1093/protein/1.2.107
10.1021/bi00180a013
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10.1016/S0021-9258(17)43463-6 / J. Biol. Chem. / Complete sequence of the staphylococcal gene encoding protein A by Uhlén M. (1984)
10.1016/S0021-9258(19)84994-3

Dates

Type	When
Created	20 years, 2 months ago (May 29, 2005, 6:36 a.m.)
Deposited	1 year, 9 months ago (Oct. 26, 2023, 8:58 p.m.)
Indexed	1 month ago (July 20, 2025, 12:27 a.m.)
Issued	30 years, 1 month ago (July 1, 1995)
Published	30 years, 1 month ago (July 1, 1995)
Published Online	21 years, 6 months ago (Feb. 3, 2004)
Published Print	30 years, 1 month ago (July 1, 1995)

Funders 0

None

BibTeX

@article{Jendeberg_1995, title={Kinetic analysis of the interaction between protein a domain variants and human Fc using plasmon resonance detection}, volume={8}, ISSN={1099-1352}, url={http://dx.doi.org/10.1002/jmr.300080405}, DOI={10.1002/jmr.300080405}, number={4}, journal={Journal of Molecular Recognition}, publisher={Wiley}, author={Jendeberg, Lena and Persson, Björn and Andersson, Roland and Karlsson, Robert and Uhlén, Mathias and Nilsson, Björn}, year={1995}, month=jul, pages={270–278} }

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