Peptide science

Peptide compound database for amino-acid sequences and chemical identifiers.

Peptides are short chains of amino acids linked by peptide bonds. This database gathers sequence, molecular mass, chemical identity, and literature for a curated set of well-studied peptides — hormones, approved peptide medicines, and classical biochemical standards.

What is recorded

The chemistry that defines a peptide.

A peptide is more than a name. Sequence, covalent shape, mass, and registry numbers are how the same substance is recognized across papers and chemical databases.

  • Amino-acid sequence

    The order of residues from N-terminus to C-terminus. Non-canonical chemistry — D-amino acids, pyroglutamate, lipidated lysines — is written beside the one-letter string.

  • Length and formula

    How many amino acids are in the chain, and the elemental composition (C, H, N, O, S) of that covalent structure.

  • Molecular weight

    Average mass in grams per mole. Peptide bonds lose water; disulfides lose two hydrogens; amides and other termini shift the mass again.

  • Chemical identifiers

    CAS Registry Numbers and PubChem compound identifiers, when they exist, so the same substance can be matched in the chemical literature.

  • Linear or cyclic

    Whether the backbone is an open chain or closed by a covalent ring — a disulfide, a thioether, or a head-to-tail peptide bond.

  • Modifications

    C-terminal amidation, N-terminal pyroglutamate, D-residues, N-methylation, and lipid conjugation change stability, charge, and receptor selectivity.

N-terminus C-terminus AA₁ −H₂O AA₂ peptide bond −H₂O Condensation joins α-carboxyl to α-amine

Peptide bonds

How amino acids become a chain.

Each peptide bond is an amide formed when the carboxyl group of one amino acid condenses with the amino group of the next, releasing water. Length counts residues, not bonds: an n-residue peptide has n − 1 peptide bonds.

Read about peptide bonds

Linear Cyclic (disulfide) Cys–Cys bridge closes a ring

Topology

Linear chains and covalent rings.

Many hormones are linear polymers. Others — oxytocin, insulin, somatostatin — are cyclic because a disulfide or another covalent link closes a ring. Classification here follows covalent topology, not whether the chain folds into a helix in water.

Linear vs cyclic

Terminal chemistry pGlu N-terminus ··· NH₂ amide Ends change mass, charge, and stability

Terminals

Why the ends of a peptide matter.

Native ribosomal peptides usually begin with a free amine and end with a free acid. Many bioactive peptides are C-terminally amidated, start as pyroglutamate, or carry other end-group chemistry that shifts mass and resists proteases.

Terminal modifications

How to look something up

Start from sequence, name, or identifier.

  1. 1

    Identify the peptide

    Enter a stretch of one-letter sequence, a common name, a CAS number, or a PubChem identifier.

  2. 2

    Restrict by chemistry

    Limit results by molecular weight, residue count, linear versus cyclic structure, and known modifications.

  3. 3

    Check the sources

    Each entry cites primary literature or a public chemical record so sequence and mass can be confirmed independently.

Scope

A reference, not a product list.

Values here are for scientific look-up. They are not medical advice and not an offer to sell any substance. Chemical identifiers link out to public registries for independent verification.