2022
Nobel Prize Class
2
Granted Patents
+135%
Tensile Strength
SGS
Independently Validated
All data independently validated by SGS Proderm, Schenefeld, Germany
02 — The Problem

Molecular damage is structural failure

Hair is an engineered material. Each fiber is built from keratin protein chains arranged in coiled-coil structures, bundled into intermediate filaments, and crosslinked by disulfide bonds — one of the strongest bond types in biological materials.

Chemical treatments — bleaching, coloring, perming — break these disulfide bonds at the cortex level, which constitutes 90% of the hair's volume. Free thiol (-SH) groups are left exposed. The internal architecture weakens progressively.

This is structural failure, not cosmetic damage. And it requires structural solutions.

03 — DISULFIDE BONDS

The architecture of strong hair

Disulfide bonds are covalent S-S linkages between cysteine residues in adjacent keratin chains. They perform three critical structural functions.

Tensile Strength

Resistance to breakage under physical stress. Disulfide crosslinks distribute mechanical load across the keratin matrix.

Elastic Modulus

The ability to flex and return to shape. Crosslinks provide restoring force — higher density means greater flexibility retention.

Structural Integrity

Overall fiber cohesion and porosity resistance. The 3D crosslinked network maintains the cortex as a continuous structural unit.

04 — Bond Breakage

What happens when bonds break

Chemical treatments cleave disulfide bonds via oxidation or reduction reactions, generating free thiol (-SH) groups on each separated cysteine residue. The consequences are measurable and progressive:

Reduced Tensile Strength
Fewer crosslinks mean less resistance to mechanical stress.

Increased E-Modulus
The fiber becomes stiffer and less elastic — it snaps rather than bending.

Higher Porosity
Loss of structural cohesion opens gaps, accelerating moisture loss.

Damage Cascade
Each broken bond increases vulnerability of neighboring bonds.

05 — THE LANDSCAPE

Why traditional approaches fall short

Three generations of hair repair technology have each advanced the conversation — but none create new covalent bonds within the cortex with independently verified efficiency.

Legacy Bond Repaid

2014 — Gen 1: Re-linking

Small molecules crosslink free thiols via Michael addition. Contested mechanism — Di Foggia et al. (2021) found no cortex-level disulfide increase via Raman spectroscopy. Competing patents describe electrostatic bonds requiring weekly reapplication. Debated durability. No independent proof of cortex activity.

Peptide-based treatment

2020 — Gen 2: Peptide Filling

Biomimetic peptides designed to integrate into damaged keratin. No peer-reviewed human efficacy trials published. Large molecules with variable cortex penetration. Fills voids rather than creating structural crosslinks.

NextGen Molecular Reconstruction

2026 — Gen 3: Molecular Reconstruction

New covalent bond creation via Nobel Prize-validated click chemistry. Independent laboratory measurement by SGS Proderm. Cortex-level structural rebuilding. Patented molecules. Non-petroleum-synthesized. ANATOMY® — Click Chemistry · Independent Validation · Granted Patents.

06 — The Breakthrough

Nobel Prize, 2022 — Click chemistry 

2022 Nobel Prize in Chemistry
Carolyn Bertozzi · Morten Meldal · K. Barry Sharpless

Click chemistry describes a class of reactions defined by modularity, wide scope, very high yields, inoffensive byproducts, and stereospecificity.

The Nobel Committee stated these reactions "brought chemistry into the era of functionalism." ANATOMY applies thiol-ene and thiol-yne reactions — formally classified as click reactions — to create new covalent bonds within damaged hair.

Unlike approaches that attempt to re-link original disulfide (S-S) bonds, ANATOMY creates entirely new carbon-sulfur (C-S) covalent bonds, forming structural bridges between damaged keratin chains.

Modular

Simple building blocks combine predictably to form complex structures.

Very High Yields

Near-complete conversion under mild conditions. 81.5% bis-adduct formation rate measured.

Mild Conditions

No harsh initiators, extreme pH, or elevated temperatures required.

Stereospecific

Reactions produce defined structural geometries — architectural precision at molecular scale.

07 — THE CHEMISTRY

Thiol recombination explained

Thiol-Ene Reaction

A free thiol group (-SH) adds across a carbon-carbon double bond (C=C), creating a new carbon-sulfur covalent bond — a thioether linkage. High yield, high rate, near-complete conversion under mild conditions. Each reaction creates one new C-S structural bridge.

Thiol-Yne Reaction

A free thiol adds across a carbon-carbon triple bond (C≡C). Each triple bond reacts sequentially with two thiol groups — doubling crosslinking density. Higher crosslinking density per reactive site → more interconnected structural networks.

Key Distinction

The result is not restoration of original S-S bonds. ANATOMY creates entirely new C-S covalent bonds — engineered for superior stability, flexibility, and permanence compared to the original biological linkages.

08 — MECHANISM OF ACTION

Four steps to molecular reconstruction

01 — Penetrate

Molecules optimized for cortex-level penetration via leave-in format. Sustained diffusion time allows migration past cuticle into the structural core.

02 — Target

Molecules find free thiol groups (-SH) on cysteine residues — the chemical signatures of broken disulfide bonds — with high specificity.

03 — React

Thiol-ene and thiol-yne click reactions proceed under mild conditions, forming stable carbon-sulfur (C-S) covalent bonds at each reactive site.

04 — Reconstruct

Bifunctional molecules bridge between separated keratin chains, creating 3D crosslinked networks that restore structural architecture.

09 — THE DATA

Measured. Not claimed.

All performance data independently measured by SGS Proderm (Schenefeld, Germany) on bleached human hair fiber samples under controlled laboratory conditions.

135%

Tensile Strength Increase (15.2 → 35.8 cN)

15%

E-Modulus Reduction (~3× greater than competitor)

81.5%

Bis-Adduct Formation Rate

2

Granted Patents (not pending)

10 — THE MOLECULES

Patented molecular architecture

Three proprietary molecules — two with granted patents — designed for targeted cortex-level reconstruction. All non-petroleum-synthesized.

Aminalyl-S — Patent Granted

Drag to rotate · Scroll to zoom

Rebuilds disulfide bond architecture, restoring strength and flexibility. Demonstrated measurable E-Modulus reduction in SGS Proderm testing.

Pro-Amino-X — Patent Granted

Drag to rotate · Scroll to zoom

Patented crosslinking salt (Salt 2, Tb-0017). Repairs internal bonds and creates protective structural networks. Reduces brittleness within the cortex.

Molecular Library

Expanding portfolio of patented crosslinking molecules, each targeting specific structural damage profiles.

Precision Targeting

Next-generation delivery systems designed for site-specific cortex repair based on individual damage mapping.

In Development

Technologies that will move molecular reconstruction from treatment to prevention. The science continues.

ANATOMY®

Explore the molecular reconstruction system

Two patented formulas. Nobel Prize-validated chemistry. Independently measured results. This is what structural hair science looks like.

Shop the System View Our Research
All claims independently validated by SGS Proderm, Schenefeld, Germany