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Structure of Nanobody Nb23
Mathias Percipalle1,2, Yamanappa Hunashal1, Jan Steyaert3,4
1Science Division, New York University Abu Dhabi, Abu Dhabi 129188, United Arab Emirates.
This study determined the solution structure of the Nb23 nanobody, revealing a dynamic CDR3 loop. This structural insight may explain differences in antigen binding compared to Nb24, aiding therapeutic antibody development.
Area of Science:
- Biochemistry
- Structural Biology
- Immunology
Background:
- Nanobodies (VHHs) are derived from camelid heavy chain-only antibodies (hcAbs).
- Nanobodies offer advantages over monoclonal antibodies (mAbs) due to smaller size and higher stability.
- Nb23 and Nb24 nanobodies inhibit amyloidogenic β2-microglobulin aggregation.
Purpose of the Study:
- To determine the solution structure of the Nb23 nanobody.
- To provide structural insights into Nb23's function and compare it with Nb24.
Main Methods:
- Nuclear Magnetic Resonance (NMR) spectroscopy for resonance assignment and chemical shift extraction.
- CS-Rosetta server and PONDEROSA for restrained modeling using NMR data.
- Molecular dynamics simulations for structural validation.
Main Results:
- The solution structure of the isolated Nb23 nanobody was successfully determined.
- Structural analysis revealed a dynamic CDR3 loop in Nb23.
Conclusions:
- The dynamic CDR3 loop of Nb23 exhibits varied orientations compared to Nb24.
- These structural differences may influence Nb23's antigen affinity and complex stability.
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