Medicinal Chemistry Intermolecular Forces PDF

Summary

This document appears to be educational material focused on intermolecular forces and their applications in medicinal chemistry. The document covers different types of forces such as dipole-dipole interactions, hydrogen bonds, and Van der Waals forces, and how they influence the interaction of molecules and specifically interactions between drugs and binding sites.

Full Transcript

dipole-dipole bonds ng and : site occurs if the...

dipole-dipole bonds ng and : site occurs if the drug the binding have dipole moments. ex : in this case , both sides have both positive charges. partially and negative target and and S In drugs the drug , binding site Id have negative positive was areas. partially # pi stacking (Stronger than : dipole-dipole interactions) this when the occurs charge on one molecule interacts with the dipole moment of another happens between aromatic rings " eX the binding y interact site can with different dipole-dipole charges on the same Molecu ↳ hydrogen bond : (weaker than ionic bond but Woals). stronger than Van der H+ takes place between a and a heteroatom (N- or 0) : ex J in this + case H is bondingto a 0- induced-dipole interactions : This happens when the charge on one molecule induces a dipole on another This also happen between can quaternary ammonium ion and aromatic ring an. ex : ion-dipole interactions : (stronger than dipole-dipole) This occurs when the charge on one molecule interacts With the dipole moment another exi this case in separate molecules with different interact with charges can the same binding site. Van der Waals interactions : (very weak This between hydrophobic of and occurs regions the drug target areas of high and low & electron densities cause temporary dipoles 2. Discuss how and why weak interactions (intermolecular forces) are used in biological reactions and state why they are important. Intermolecular forces are used in biological reactions by driving the function structure and dynamics of , biomolecules. These reactions important are because they but reversed. are strong weak enough to be and They also allow for specificity energy efficiency.. 3 Describe and identify hydrogen bonds including portions of molecules that can act as hydrogen bond donors, hydrogen bond acceptors, or both. Hydrogen bonds take place between an electron-deficient hydrogen and an electron-rich heteroatom Lo or N) The He called the bond donor (HBD). is hydrogen The 0- or N- is called a hydrogen bond acceptor (HBA) 4 Amino acids likely to interact through specific intermolecular forces hydrogen bonding: Serine asparagine tyrosine · , , ionic bonding : lysine arginine histidine, · , , aspartic acid glutamic acid , hydrophobic interactions : alanine valine leucine , isoleucine , · , , methionine , phenylalanine , tryptophan proline , der Waals van forces: phenylalanine leucine , valine · , : pi stacking phenylalanine tyrosine tryptophann lysine · , , , argininee , · disulfide bonds: cysteine