lactambinding

Lactambinding is a term used to describe the interaction between lactam-containing molecules and biological macromolecules, such as enzymes or receptors. Lactams are cyclic amides found in various natural products and drugs, including four-membered beta-lactams. The study of lactambinding focuses on binding affinity, specificity, and kinetic parameters, as well as the structural basis for how the lactam ring engages its target.

Binding can proceed through non-covalent interactions such as hydrogen bonds to the lactam carbonyl or amide nitrogen, electrostatic contacts with active-site residues, and hydrophobic fitting within binding pockets. In some cases, lactams act as covalent inhibitors; a prominent example is beta-lactam antibiotics, which covalently acylate a nucleophilic residue in penicillin-binding proteins, leading to enzyme inactivation.

Prominent examples and contexts include beta-lactam antibiotics binding to penicillin-binding proteins in bacteria, and other lactam-containing scaffolds designed to inhibit proteases or hydrolases. Understanding lactambinding is important for drug design, as ring strain and electronic properties influence reactivity and selectivity, and resistance mechanisms can alter the binding environment.

Research approaches in lactambinding include structural biology to determine binding modes, biophysical assays to measure affinity and kinetics, and computational methods to predict binding and guide optimization. Knowledge of lactambinding supports the development of new inhibitors with improved potency and reduced off-target effects.