mAb lead optimization
Have a lead antibody, but need humanization or improvement of
affinity or function?
Abwiz Bio is a San Diego–based antibody engineering and discovery CRO. We raise antibody affinity from nanomolar to picomolar KD (STEM™, up to 1,300-fold), humanize mouse, rat, rabbit and camelid antibodies with retained affinity, and discover rabbit monoclonal antibodies by phage display against GPCRs, ion channels, phospho-sites and other difficult targets.
Why Leading Biotechs Choose Abwiz Bio
Founded 2012 · PhD-led scientific team · patented WizAmp™ library construction (US Pat. 9,890,414)
1,338×
Affinity Improvement
2.8×
More Potent Than Infliximab
15/15
Humanization Success
Featured case study
We made infliximab more potent and more developable — and published the step that did not work first time
Humanized onto human germline frameworks, matured with STEM™, then re-engineered by targeted CDR substitution once developability profiling exposed a self-association liability that maturation alone had not removed.
2.8×
more potent than infliximab
4.8×
more potent than adalimumab
19.33 → −1.67
AC-SINS Δλmax (nm)
>1800×
faster off-rate at pH 5.8
Read the case study → See all case studies →
Free 30-minute call with the PhD scientist who would run the work · Initial feasibility assessment within two business days · NDA available before you disclose your target Talk to a scientist →
Antib Ther 2023 · all eight authors are Abwiz Bio · 21 SARS-CoV-2 variants tested head to head
What happens when your target mutates out from under the antibody
We rebuilt a neutralizing antibody that had stopped working, and it went from covering 7 of 21 variants to covering all 21 — including eight that a clinical-stage therapeutic antibody no longer touched.
21 / 21
Variants neutralized
After re-maturation, every variant in the panel
≤7 pM
KD on BQ.1.1
Parent antibody had no measurable binding
~1,000×
Slower off-rate
On-rate barely moved — it stopped letting go
Worth saying plainly: on the variants bebtelovimab still covers, it is the more potent antibody — 5.3 ng/mL against BA.5 versus our 9.4. The engineered antibodies win on breadth, not on peak potency. For a therapeutic program, that is usually the axis that decides whether the asset survives.
What this means for a campaignThe 21–24 mutations that produced this were not found by walking one CDR at a time — none of the winning sequences appeared when single-CDR or separately combined libraries were screened. Staged selection is what reached them, which is the same three-stage design we run in STEM™ affinity maturation and functional and neutralizing discovery.
Entzminger KC, Fleming JK, Entzminger PD, Espinosa LY, Samadi A, Hiramoto Y, Okumura SCJ, Maruyama T. Rapid engineering of SARS-CoV-2 therapeutic antibodies to increase breadth of neutralization including BQ.1.1, CA.3.1, CH.1.1, XBB.1.16, and XBB.1.5. Antibody Therapeutics 2023;6(2):108–118.
All eight authors: Abwiz Bio, Inc., San Diego, California.
Published mechanism
Why our antibodies work on the real protein, not just the peptide
A modification-specific antibody can look perfect against a synthetic peptide and still fail on the intact protein. Our scientists have published the crystal structures that explain when that happens and why. These are those papers, written up so you can get the answer without reading the paper.
0.90 nM failed · 14 nM and 54 nM worked
Why the highest-affinity clone can fail on a Western blot
In a panel of methyl-lysine antibodies against MAP3K2 K260me3, the tightest binder gave only a faint band while two much weaker clones detected full-length protein cleanly. Four crystal structures explain it: the failing clones were binding the peptide’s C-terminal carboxyl group, which does not exist in the intact protein.
Read the explainer →~300× discrimination · J Biol Chem 2024
How a phospho-specific antibody tells the two forms apart
Two rabbit monoclonals against phospho-Akt (pSer473). One binds the phosphopeptide about 300-fold more tightly than the unmodified peptide; the other shows no detectable binding to the unmodified form at all. Crystal structures, ITC alanine scanning and six microseconds of molecular dynamics show what makes the difference.
Read the explainer →0.81 nM KD · PDB 9J8A
Recognizing a modification down to which residue carries it
An antibody that binds sulfated CCR5 at nanomolar affinity with no measurable binding to the unsulfated peptide — and that distinguishes which tyrosine carries the sulfate. The solved structure is deposited as PDB 9J8A.
Read the explainer →All 25 peer-reviewed publications, including the eight we have written up in full →
Abwiz Bio Therapeutic
Antibody Development Plan
Accelerate the development of therapeutic lead candidates with our end-to-end solutions. Every step of our process is fully optimized and tailored to deliver exactly what you need.
STEP 1
Immunization
STEP 2
Library
Construction
WizAmp™
STEP 3
Panning &
Screening
STEP 4
Recombinant
IgG production
STEP 5
Humanization
STEP 6
Affinity Maturation
and Optimization
Stem™