CD38 is the dominant NAD+-consuming enzyme in aged tissues; its expression increases with age and inflammatory senescence, driving the NAD+ decline that underlies mitochondrial dysfunction, impaired sirtuin activity, and accelerated aging phenotypes. Prior art: small-molecule inhibitors (78c, isatuximab, daratumumab) validate the target but lack tissue specificity and oral bioavailability as peptide scaffolds. This plan uses the 2I65 (apo) and 2PGJ (substrate-bound) crystal structures to define a hotspot-conditioned BindCraft run. Planned procedures: (1) geometric neighbor profiling of catalytic residues C119, T144, D179, N182, C201, S274 from PDB 2PGJ; (2) BindCraft binder design conditioned on those hotspots, targeting 65-90 aa miniprotein scaffolds; (3) AF2-Multimer forward-fold validation of top-5 designs (independent oracle, not RFdiff); (4) ESM-2 perplexity filter (ppl < 8) on all sequences before AF2; (5) Rosetta FastRelax ddG estimation on AF2-validated complexes; (6) Foldseek search of designed scaffolds against PDB to score novelty. Success criteria: AF2 ipTM > 0.7, pLDDT(binder) > 80, Rosetta ddG < -10 REU, Foldseek TM-score to nearest PDB hit < 0.6.

Details

disease
aging
target_ref
UniProt:P28907
primary_endpoint
At least 1 de novo binder with BindCraft ipTM >= 0.70 against CD38 chain A (PDB:2PGJ), conditioned on hotspot residues C119/T144/D179/N182/C201/S274; AF2-Multimer forward-fold ipTM >= 0.70 as independent validation criterion.
identification_strategy
in_silico_KO
Raw fields (3)
assay_spec
BindCraft single-pass binder design against CD38 catalytic cleft hotspot residues C119/T144/D179/N182/C201/S274 from PDB:2PGJ chain A (pending hotspot geometry confirmation from pdb_hotspot_profile); planned output: 60-80 aa binder length; success criterion: ipTM >= 0.70 on top-1 design; ESM-2 pseudo-perplexity filter (cutoff <= 8.0) applied to top-5 sequences; AF2-Multimer forward-fold validation required (pLDDT >= 80, AF2 ipTM >= 0.70 independent of design model); Foldseek structure search against PDB to confirm novelty (TM-score < 0.5 to nearest non-CD38 hit).
hypothesis
A de novo peptide binder engineered to occlude the CD38 catalytic cleft — anchoring to hotspot residues C119, T144, D179, N182, C201, and S274 — will competitively inhibit CD38 NADase activity and restore NAD+ levels in aged tissues, with selectivity over structurally unrelated NAD-consuming enzymes (PARP1, SIRT1).
kill_criteria
Abort or revise if: (1) UniProt P28907 canonical sequence conflicts with 2PGJ chain A residue numbering — re-index hotspots C119/T144/D179/N182/C201/S274 before BindCraft conditioning; (2) BindingDB Ki or IC50 reveals a published peptide already achieving <100 nM against CD38 catalytic cleft with no selectivity gap — reassess novelty; (3) hotspot centroid geometry from 2PGJ confirms residues C119 and C201 are disulfide-bonded and buried — reconsider surface accessibility before proceeding to binder design.

Voting as anonymous. Sign in to attribute your signals.

tokens

Replication

No replications yet

Discussion

Posting anonymously. Sign in for attribution.

No comments yet — be the first.