Curated reading path
Use D-amino acids, N-methylation and conformational constraints to balance activity, stability, permeability and manufacturability.
6 published articles in recommended order
Non-natural amino acids can improve the stability, conformation, membrane permeability, and pharmacokinetic properties of peptide drugs, among which D-amino acids and N-methyl amino acids have become important tools in modern peptide drug development.
N-methyl amino acids can improve the membrane permeability, metabolic stability, and developability of peptide drugs by modulating the number of hydrogen-bond donors, polar surface area, conformational preferences, and modes of protease recognition, making them important tools in the design of cyclic peptides and oral peptide drugs.
Unnatural amino acids are not merely a simple expansion of the natural amino acid alphabet; rather, they are design variables capable of altering backbone geometry, side-chain interactions, conformational preferences, and synthetic routes. Their rational application requires starting from the specific bottlenecks of existing peptides and making multi-objective trade-offs among activity, stability, permeability, solubility, and manufacturability.
Learn when a linear peptide should be cyclized and how cyclic peptide design compares lactam, disulfide, and head-to-tail cyclization strategies while accounting for AI-guided structural review, synthesizability, and practical peptide synthesis.
AI peptide optimization can balance stability and solubility around an existing parent peptide. Learn how NCAAs, D-amino acids, N-methylation, cyclization, synthesizability, and practical peptide synthesis shape candidate selection.
AI peptide design can generate candidates quickly, but biological scores do not guarantee practical synthesis or purification. This article explains how peptide synthesizability, SPPS, noncanonical amino acids, cyclic peptides, purification difficulty, and practical peptide synthesis should shape candidate selection.