Pioneering the future of research.
20 Aminos supplies the global scientific community with uncompromising quality and high-purity research peptides, verified, documented, and ready for the bench.

The alphabet
Expand any residue for IUPAC codes, free-form molecular formula, side chain, and a short structural note. Residue drawings will land in a later pass.
AlanineAla · A · Nonpolar
- Formula
- C₃H₇NO₂
- Side chain (R)
- –CH₃
A compact nonpolar residue with a methyl side chain. Common in peptide cores where small hydrophobic packing is preferred.
ArginineArg · R · Basic
- Formula
- C₆H₁₄N₄O₂
- Side chain (R)
- –(CH₂)₃–NH–C(NH₂)=NH
A basic residue with a guanidinium side chain that remains protonated under typical laboratory buffer conditions.
AsparagineAsn · N · Polar
- Formula
- C₄H₈N₂O₃
- Side chain (R)
- –CH₂–CONH₂
A polar amide side chain that participates in hydrogen bonding and is a common site of N-linked glycosylation motifs in proteins.
Aspartic acidAsp · D · Acidic
- Formula
- C₄H₇NO₄
- Side chain (R)
- –CH₂–COOH
An acidic residue whose carboxylate side chain is typically deprotonated near physiological pH in aqueous buffer.
CysteineCys · C · Special geometry
- Formula
- C₃H₇NO₂S
- Side chain (R)
- –CH₂–SH
A thiol-containing residue that can form disulfide bonds (cystine) and is widely used for site-specific chemistry in research peptides.
GlutamineGln · Q · Polar
- Formula
- C₅H₁₀N₂O₃
- Side chain (R)
- –(CH₂)₂–CONH₂
A polar amide homolog of asparagine with a longer side chain, frequent in solvent-exposed loops of peptide structures.
Glutamic acidGlu · E · Acidic
- Formula
- C₅H₉NO₄
- Side chain (R)
- –(CH₂)₂–COOH
An acidic residue with a carboxylate side chain one methylene longer than aspartate; common in salt-bridge networks.
GlycineGly · G · Special geometry
- Formula
- C₂H₅NO₂
- Side chain (R)
- –H
The smallest amino acid (hydrogen side chain). It confers backbone flexibility and is frequent in tight turns.
HistidineHis · H · Basic
- Formula
- C₆H₉N₃O₂
- Side chain (R)
- –CH₂–imidazole
An imidazole side chain with a pKa near neutral pH, making it useful for metal coordination and acid–base chemistry in model systems.
IsoleucineIle · I · Nonpolar
- Formula
- C₆H₁₃NO₂
- Side chain (R)
- –CH(CH₃)CH₂CH₃
A branched hydrophobic residue (β-branched). Sterically constrained backbone angles relative to leucine.
LeucineLeu · L · Nonpolar
- Formula
- C₆H₁₃NO₂
- Side chain (R)
- –CH₂CH(CH₃)₂
A branched hydrophobic residue common in amphipathic helices and hydrophobic cores of folded peptides.
LysineLys · K · Basic
- Formula
- C₆H₁₄N₂O₂
- Side chain (R)
- –(CH₂)₄–NH₂
A basic residue with a primary amine side chain, often used for conjugation and labeling chemistry in research materials.
MethionineMet · M · Nonpolar
- Formula
- C₅H₁₁NO₂S
- Side chain (R)
- –(CH₂)₂–S–CH₃
A sulfur-containing nonpolar residue; the genetic start codon encodes methionine in standard translation initiation.
PhenylalaninePhe · F · Aromatic
- Formula
- C₉H₁₁NO₂
- Side chain (R)
- –CH₂–C₆H₅
An aromatic hydrophobic residue with a benzyl side chain; contributes UV absorbance near 260 nm in peptide spectra.
ProlinePro · P · Special geometry
- Formula
- C₅H₉NO₂
- Side chain (R)
- pyrrolidine ring
A cyclic secondary amine that kinks the backbone; often breaks α-helices and defines turn geometry in peptides.
SerineSer · S · Polar
- Formula
- C₃H₇NO₃
- Side chain (R)
- –CH₂OH
A small polar residue with a hydroxymethyl side chain; a common hydrogen-bond donor/acceptor in peptide structures.
ThreonineThr · T · Polar
- Formula
- C₄H₉NO₃
- Side chain (R)
- –CH(OH)CH₃
A β-branched polar residue with a secondary alcohol; side-chain chirality adds steric constraint versus serine.
TryptophanTrp · W · Aromatic
- Formula
- C₁₁H₁₂N₂O₂
- Side chain (R)
- –CH₂–indole
The largest standard aromatic residue (indole). Strong UV absorbance near 280 nm makes it a useful spectroscopic handle.
TyrosineTyr · Y · Aromatic
- Formula
- C₉H₁₁NO₃
- Side chain (R)
- –CH₂–C₆H₄OH
An aromatic residue with a phenolic side chain; UV-active and often involved in hydrogen-bond networks at interfaces.
ValineVal · V · Nonpolar
- Formula
- C₅H₁₁NO₂
- Side chain (R)
- –CH(CH₃)₂
A β-branched hydrophobic residue that favors extended backbone conformations in peptide secondary structure.
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To be the globally trusted standard for research peptides, driving innovation in laboratory science one fully documented lot at a time.
What we stand for
What sets 20 Aminos apart.
Three commitments that guide every release in the 20 Aminos catalog.
Uncompromising quality
Every peptide is produced to 99%+ purity, your research data stays reliable and reproducible.
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Independent HPLC and ESI-MS reports accompany every batch, no exceptions, no shortcuts.
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Quality assurance
Research confidence.
From raw material sourcing to final lyophilization, 20 Aminos maintains rigorous environmental controls, temperature, humidity, particulate, so every batch meets exacting specifications.
Multi-stage testing, HPLC purity analysis, ESI-MS verification, ensures that what’s on the label is exactly what’s in the vial. Authenticity and precision, every release.
Documentation
Every batch is verified.
Comprehensive third-party testing documentation ships with every product, full chromatograms, full spectra, full chain of custody.
Chromatography
Purity documentation supporting batch-level transparency and peer review.
Mass spectrometry
Verification confirming product identity and lot-specific batch details.
Third-party docs
Every product ships with comprehensive documentation for full research review.
Certificate of analysis
Lot-specific COA, methods, raw data, validation criteria, attached to every order.
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Documentation you can check.
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Products are intended for in vitro research use only. Not for human or veterinary use. Not for diagnostic or therapeutic purposes.
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