School of Peptide Chemistry

15 published lessons · Peptide Chemistry Foundations

Lesson order

1. Lesson 1 · 22–28 min · Beginner

   What Is a Peptide?

   An evidence-based introduction to peptides, amino acids, peptide bonds, sequence, structure, and the differences among peptides, polypeptides, and proteins.

2. Lesson 2 · 30–38 min · Beginner–Intermediate

   Amino Acids: Structure, Classification, and Chemical Behavior

   A detailed guide to amino-acid structure, side-chain classes, stereochemistry, ionization, and the chemical features that shape peptide behavior.

3. Lesson 3 · 28–34 min · Intermediate

   Peptide Bonds: Formation, Geometry, and Chemical Stability

   An in-depth explanation of peptide-bond formation, resonance, planarity, cis-trans behavior, hydrolysis, and analytical implications.

4. Lesson 4 · 26–32 min · Intermediate

   Primary Structure: How Sequence Defines Peptide Identity

   A technical guide to peptide sequence, residue numbering, terminal modifications, sequence variants, molecular mass, and identity confirmation.

5. Lesson 5 · 30–38 min · Intermediate–Advanced

   Higher-Order Peptide Structure

   An accessible technical guide to peptide conformation, alpha helices, beta structures, turns, disorder, cyclization, aggregation, and structural analysis.

6. Lesson 6 · 26–32 min · Intermediate

   Peptide Molecular Weight and Mass Calculation

   Learn how peptide molecular weight is calculated, why monoisotopic and average mass differ, and how termini, disulfides, salts, and modifications affect expected mass.

7. Lesson 7 · 28–34 min · Intermediate

   Peptide Charge, pKa, and Isoelectric Point

   Understand how ionizable groups, pH, pKa, and isoelectric point determine peptide charge, solubility, electrophoretic behavior, and analytical performance.

8. Lesson 8 · 26–32 min · Intermediate

   Peptide Hydrophobicity and Molecular Interactions

   Explore how residue composition, sequence, solvent exposure, and conformation control peptide hydrophobicity, reversed-phase retention, aggregation, and surface adsorption.

9. Lesson 9 · 32–40 min · Intermediate–Advanced

   Peptide Solubility: Chemical Drivers and Analytical Considerations

   Learn how pH, charge, hydrophobicity, concentration, ionic strength, temperature, and physical state determine peptide solubility and analytical recovery.

10. Lesson 10 · 28–36 min · Intermediate–Advanced

    Amphipathic Peptides and Interfacial Behavior

    Understand how peptides containing distinct hydrophobic and hydrophilic regions interact with water, membranes, interfaces, chromatographic systems, and one another.

11. Lesson 11 · 34–42 min · Intermediate–Advanced

    Solid-Phase Peptide Synthesis (SPPS)

    Understand the core logic of solid-phase peptide synthesis, including resin attachment, repetitive coupling and deprotection cycles, washing, sequence extension, and common process risks.

12. Lesson 12 · 34–42 min · Advanced

    Protecting Groups in Peptide Synthesis

    Learn why peptide synthesis requires temporary and side-chain protecting groups, how orthogonality works, and how protection strategy affects yield, selectivity, impurity formation, and final deprotection.

13. Lesson 13 · 36–44 min · Advanced

    Peptide Coupling Chemistry

    Understand how amino-acid carboxyl groups are activated for peptide-bond formation, how coupling efficiency is assessed, and how racemization, incomplete reaction, and reagent choice influence quality.

14. Lesson 14 · 34–42 min · Advanced

    Peptide Cleavage and Global Deprotection

    Learn how completed peptides are released from solid supports, how side-chain protecting groups are removed, why scavengers are used, and how cleavage conditions shape the crude impurity profile.

15. Lesson 15 · 38–46 min · Advanced

    Peptide Purification by Preparative Chromatography

    Understand how crude peptide mixtures are separated using preparative chromatography, how fractions are evaluated and pooled, and how purity, recovery, resolution, and scale are balanced.