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Fmoc-Gly-Gly-OH is a dipeptide derivative featuring an Fmoc-protected glycine residue coupled to a second glycine via an amide bond, resulting in the structural formula Fmoc-NH-CH₂-CO-NH-CH₂-COOH. The molecule contains no chiral centers, as glycine is achiral. The dipeptide backbone is highly flexible, making Fmoc-Gly-Gly-OH an ideal building block for constructing peptide‑based linkers.

Fmoc-Asp(OtBu)-OH is an Fmoc-protected L-aspartic acid derivative featuring a tert-butyl (OtBu) protecting group on the side chain β‑carboxyl group. Structurally, the molecule consists of an L-aspartic acid core with the primary amine protected by a 9-fluorenylmethoxycarbonyl (Fmoc) group — the standard base-labile protecting group for solid-phase peptide synthesis (SPPS) — and the side chain carboxylic acid protected as a tert-butyl ester.

Fmoc-D-Leu-OH (N-[(9H-fluoren-9-ylmethoxy)carbonyl]-D-leucine) is an N-Fmoc protected form of D-leucine, the non-natural enantiomer of the essential branched-chain amino acid L-leucine. The molecular structure features a 9-fluorenylmethyloxycarbonyl (Fmoc) group attached to the α-amino group of D-leucine, while the carboxylic acid remains free for peptide bond formation.

Fmoc-Dab(Boc)-OH (N-[(9H-fluoren-9-ylmethoxy)carbonyl]-N‘-tert-butoxycarbonyl-L-2,4-diaminobutyric acid) is an orthogonally protected derivative of the non‑proteinogenic amino acid L‑2,4-diaminobutyric acid (Dab). The structure comprises a base‑labile 9‑fluorenylmethyloxycarbonyl (Fmoc) group protecting the α‑amine, and an acid‑labile tert‑butoxycarbonyl (Boc) group protecting the γ‑amine side chain. This orthogonal protection scheme—Fmoc on the α‑amine and Boc on the γ‑amine—enables selective, sequential deprotection and functionalization of two distinct amine positions within a single amino acid building block.

Fmoc-Thi-OH is an Fmoc-protected unnatural amino acid featuring a thiophene heterocycle as the side chain. Structurally, the molecule comprises a fluorenylmethyloxycarbonyl (Fmoc) group protecting the α-amino functionality, a central alanine-derived chiral center, and a 2-thienyl group at the β-position. The thiophene ring serves as a sulfur-containing aromatic bioisostere of the phenylalanine benzene ring, offering similar electronic properties but with distinct polarizability and hydrogen-bonding characteristics.

Fmoc-Asn(Trt)-OH is a fully protected L-asparagine derivative designed specifically for solid‑phase peptide synthesis. The α‑amino group is protected with the Fmoc group for chain elongation control, while the amide side chain of asparagine is protected with a trityl (triphenylmethyl, Trt) group. This orthogonal protection strategy is critical for asparagine, as its unsubstituted side chain amide can undergo undesirable side reactions including dehydration to cyanoalanine during peptide assembly.