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Peptide chemistry fundamentals: amino acids, chirality and sequence notation.
What makes a medicine a peptide drug, how many are approved, how insulin, octreotide and the GLP-1 drugs were engineered and made, and how they differ from research peptides.
Histidine structure explained: formula and masses, the imidazole side chain and its two nitrogens, tautomers, a pKa near 6, and how histidine binds copper and nickel.
Glycine structure and proline structure explained: why glycine is achiral, why proline is not an imino acid, cis-trans proline isomerization and split HPLC peaks.
N-acetyl peptides explained: the fixed 42 Da mass shift, why an acetate salt is not N-acetylation, and what is actually published.
Peptide sequence notation decoded: H-/-OH and Ac-/-NH2 termini, cyclo and disulfide bridges, non-standard residues and salt forms, plus what end caps do.
Peptide molecular weight explained: calculating it from the sequence, end groups and disulfides, why salt forms weigh more, and how to check a certificate.
Peptides vs small molecules: size, synthesis, stability, analysis and how each reaches its target, and why a peptide catalogue also lists non-peptides.
Amino acid analysis explained: acid hydrolysis, derivatization and quantitation, which residues are lost, and how AAA compares with CHN, qNMR and UV.
What dipeptides, tripeptides and oligopeptides are, how short peptides are named and counted, and examples from glutathione and GHK-Cu to KPV, TRH and aspartame.
What cell-penetrating peptides are, how the Tat and penetratin discoveries happened, why the 2003 fixation artefact reset the field, why endosomal escape is still the bottleneck, and where CPPs stand today.
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