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Antibody Affinity Maturation: Enhancing Binding Affinity via Mutation and Selection, Essays (university) of Biology

4th Military Medical UniversityBiology

Antibody affinity maturation is a process to enhance the binding affinity of an antibody to an antigen. In vitro affinity maturation can be achieved through mutation and selection. Creative biolabs offers extensive experience in antibody affinity maturation using scfv format and monovalent display phagemid system. Two methods, untargeted mutagenesis and oligonucleotide-directed mutagenesis, are employed to construct random or defined sub-libraries to introduce mutants. Subsequent library screening using surface-panning and solution-sorting strategies selects antibody mutants with high affinity.

Typology: Essays (university)

2018/2019

Uploaded on 03/07/2019

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antibody affinity maturation service
s
•Affinity maturation is the process to improve antibody affinity for an a
ntigen.Invivo, natural affinity maturation by the immune system take
s place by somatic hypermutation and clonal selection. Invitro, in the
laboratory affinity maturation, can be obtained by mutation and selec
tion.
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antibody affinity maturation service

s

  • (^) Affinity maturation is the process to improve antibody affinity for an a

ntigen. In vivo , natural affinity maturation by the immune system take

s place by somatic hypermutation and clonal selection. In vitro , in the

laboratory affinity maturation, can be obtained by mutation and selec

tion.

  • (^) Creative Biolabs has gained extensive experience in antibody affinity maturatio

n. We usually take scFv as the antibody format in affinity maturation. Also, a m

onovalent display phagemid system is used to reduce the avidity effects during

antigen-binding screening. We also provide affinity maturation services for sing

le domain antibodies. Two methods, untargeted mutagenesis and oligonucleoti

de-directed mutagenesis, are employed to construct random or defined sub-lib

raries to introduce a large number of mutants of the original antibody. Antibod

y binders of higher affinity are then selected by increasing the screening string

ency. By constructing a series of sub-libraries of a scFv/Fab antibody, our propri

etary protocol allows increase of the affinity of the scFv antibodies from 10 -9 t

o 10 -10. We have successfully obtained a scFv antibody that has an extremely

high affinity of 10 -12, whose binding to the antigen is essentially irreversible.

  • (^) Subsequent library screening will fish out the antibody mutants that have high affini ty. Two library screening strategies are available. In the first "surface-panning" strat egy, decreasing concentrations of antigen is surface immobilized. In the second "sol ution-sorting" strategy, in which a labeled antigen in solution is used, we have two approaches, selection based on the equilibrium constant (Kd) and selection based o n binding kinetics. In the first approach, sub-library phage is incubated with biotinyl ated antigen at controlled concentrations and bound phages are captured by immo bilized NeutrAvidin. Selection based on binding kinetics is also termed off-rate (Kof f) selection, in which phage population is allowed to saturate the labeled antigen be fore a large molar excess of unlabeled antigen is added to the mix for controlled per iods of time. This allows the selection of mutant antibodies that have slower off-rat es. Since a reduction in Koff usually results in a higher affinity, this selection approa ch singles out antibody variants with improved Kd.