Lauren Boucher
Research Subjects
Lauren Boucher has a total of 267 co-authors. Here are the top co-authors by number of shared publications:
Amelie Forest
24 shared publicationsAndreas Sonyi
24 shared publicationsAnthony L. Pennello
24 shared publicationsCarmine Carpenito
24 shared publications- Colleen Burns
Lakeland Ctr Fetal Alcohol Spectrum Disorder, Cold Lake, AB, Canada
24 shared publications Dale L. Ludwig
24 shared publications
Latest Publications
- Open Access
- 19 April 2023
- Published by Taylor & Francis in mAbs
- Vol. 15 (1) , 2195517
“Stapling” scFv for multispecific biotherapeutics of superior properties
Single-chain fragment variable (scFv) domains play an important role in antibody-based therapeutic modalities, such as bispecifics, multispecifics and chimeric antigen receptor T cells or natural killer cells. However, scFv domains exhibit lower stability and increased risk of aggregation due to transient dissociation (“breathing”) and inter-molecular reassociation of the two domains (VL and VH). We designed a novel strategy, referred to as stapling, that introduces two disulfide bonds between the scFv linker and the two variable domains to minimize scFv breathing. We named the resulting molecules stapled scFv (spFv). Stapling increased thermal stability (Tm) by an average of 10°C. In multiple scFv/spFv multispecifics, the spFv molecules display significantly improved stability, minimal aggregation and superior product quality. These spFv multispecifics retain binding affinity and functionality. Our stapling design was compatible with all antibody variable regions we evaluated and may be widely applicable to stabilize scFv molecules for designing biotherapeutics with superior biophysical properties.
- 19 April 2023
- Published by Taylor & Francis in mAbs
- Vol. 15 (1) , 2195517
Open Access“Stapling” scFv for multispecific biotherapeutics of superior properties
Single-chain fragment variable (scFv) domains play an important role in antibody-based therapeutic modalities, such as bispecifics, multispecifics and chimeric antigen receptor T cells or natural killer cells. However, scFv domains exhibit lower stability and increased risk of aggregation due to transient dissociation (“breathing”) and inter-molecular reassociation of the two domains (VL and VH). We designed a novel strategy, referred to as stapling, that introduces two disulfide bonds between the scFv linker and the two variable domains to minimize scFv breathing. We named the resulting molecules stapled scFv (spFv). Stapling increased thermal stability (Tm) by an average of 10°C. In multiple scFv/spFv multispecifics, the spFv molecules display significantly improved stability, minimal aggregation and superior product quality. These spFv multispecifics retain binding affinity and functionality. Our stapling design was compatible with all antibody variable regions we evaluated and may be widely applicable to stabilize scFv molecules for designing biotherapeutics with superior biophysical properties.