| dc.creator | TREMARIN, BEATRIZ | |
| dc.creator | YOKAICHIYA, FABIANO | |
| dc.creator | KELLERMANN, GUINTHER | |
| dc.creator | FRANCO, MARGARETH K.K.D. | |
| dc.creator | STORSBERG, JOACHIM | |
| dc.date | 2021 | |
| dc.date | 2022-03-29T15:50:02Z | |
| dc.date | 2022-03-29T15:50:02Z | |
| dc.date.accessioned | 2023-09-28T14:21:41Z | |
| dc.date.available | 2023-09-28T14:21:41Z | |
| dc.identifier | 1867-2450 | |
| dc.identifier | http://repositorio.ipen.br/handle/123456789/32882 | |
| dc.identifier | 6 | |
| dc.identifier | 13 | |
| dc.identifier | 10.1007/s12551-021-00845-2 | |
| dc.identifier | Sem Percentil | |
| dc.identifier | 90.00 | |
| dc.identifier.uri | https://repositorioslatinoamericanos.uchile.cl/handle/2250/9003101 | |
| dc.description | INTRODUCTION
Antibodies are used by jawed vertebrates for defense against invading
pathogens. Usage of those versatile tools in a plethora of settings in clinics
and biomedical sciences hinges on functionalization strategies that retain
native antibody reactivity. To this date, antibody functionalization is performed
by trial and error.
OBJECTIVES
We aim to reduce costs by providing general principles to allow the full
spectrum of antibody functionalization by correlating functionalized antibody
reactivity to cognate antigen by small angle neutron scattering,
SANS, measurements and mathematical modeling of antibody and
antibody-antigen super-complexes, obtained by titration experiments.
MATERIALS AND METHODS
For this research we have used for as antibody pure goat anti rabbit
immunoglobulin, and for the antigen, pure Horseradish Peroxidase
Preliminary results show that the systems (antibody and
antibody-antigen complexes) do not change in the range of a temperature
related to storage temperature (25?? C), body temperature (37?? C) and 40??
C.
DISCUSSION AND RESULTS
These results will give us the pair distribution function of these systems
and the results will be viewed in light of published precedence to highlight
areas where future effort is needed to refine such versatile tools and
improve their production. However, between the antibody and the complexes
structure, different conformations were observed. The antibody
has a globular structure with a radius of gyration around 33 ??, and the
complexes display an elongated cylindrical shape with radius of gyration
around 63 ??.
CONCLUSION
This study shows how the scattering techniques (SANS) can provide
useful information about the conformation of the antibody and
antibody-antigen formation and help to shed light in the understanding
the physical, chemical, and structural changes on the organization of these
important antibody functionalization for the immunological system. | |
| dc.format | 1301-1301 | |
| dc.relation | Biophysical Reviews | |
| dc.rights | openAccess | |
| dc.source | IUPAB International Congress, 20th; SBBf Congress, 45th; Annual Meeting of SBBq, 50th, October 4-8, 2021, S??o Paulo, SP | |
| dc.title | Improvement of the methodological strategies to product functionalizes antibodies using Small Angle Neutron Scattering (SANS) | |
| dc.type | Resumos em peri??dicos | |
| dc.coverage | I | |
