EFFECT OF INTRAMOLECULAR DISPERSION INTERACTIONS ON THE CONFORMATIONAL PREFERENCES OF MONOTERPENOIDS

2017 ◽  
Author(s):  
Donatella Loru ◽  
M. Sanz ◽  
Jackson Tang ◽  
Andreia Santos ◽  
Annalisa Vigorito
Keyword(s):  
Dispersion Interactions ◽  
Conformational Preferences

Novel simulation model for many-body multipole dispersion interactions

1998 ◽  
Vol 94 (3) ◽  
pp. 417-433 ◽  
Author(s):  
MARTIN VAN DER HOEF ◽  
PAUL MADDEN
Keyword(s):  
Simulation Model ◽  
Dispersion Interactions ◽  
Many Body

NMR spectroscopy in the conformational analysis of peptides: an overview

2020 ◽  
Vol 27 ◽  
Author(s):  
Marian Vincenzi ◽  
Flavia Anna Mercurio ◽  
Marilisa Leone
Keyword(s):  
Nmr Spectroscopy ◽  
Protein Interactions ◽  
3D Structure ◽  
Theoretical Background ◽  
Triple Resonance ◽  
Protein Protein Interactions ◽  
Nmr Studies ◽  
Conformational Preferences ◽  
Dynamic Perspective ◽  
Nmr Methods

Background: NMR spectroscopy is one of the most powerful tools to study the structure and interaction properties of peptides and proteins from a dynamic perspective. Knowing the bioactive conformations of peptides is crucial in the drug discovery field to design more efficient analogue ligands and inhibitors of protein-protein interactions targeting therapeutically relevant systems. Objective: This review provides a toolkit to investigate peptide conformational properties by NMR. Methods: Articles cited herein, related to NMR studies of peptides and proteins were mainly searched through Pubmed and the web. More recent and old books on NMR spectroscopy written by eminent scientists in the field were consulted as well. Results: The review is mainly focused on NMR tools to gain the 3D structure of small unlabeled peptides. It is more application-oriented as it is beyond its goal to deliver a profound theoretical background. However, the basic principles of 2D homonuclear and heteronuclear experiments are briefly described. Protocols to obtain isotopically labeled peptides and principal triple resonance experiments needed to study them, are discussed as well. Conclusion: NMR is a leading technique in the study of conformational preferences of small flexible peptides whose structure can be often only described by an ensemble of conformations. Although NMR studies of peptides can be easily and fast performed by canonical protocols established a few decades ago, more recently we have assisted to tremendous improvements of NMR spectroscopy to investigate instead large systems and overcome its molecular weight limit.

Conformational Preferences of Chiral Acyclic Homooligomeric β2,2-Peptides

2014 ◽  
Vol 14 (10) ◽  
pp. 1225-1234 ◽  
Author(s):  
Fernando Rodriguez ◽  
Francisco Corzana ◽  
Alberto Avenoza ◽  
Jesus Busto ◽  
Jesus Peregrina ◽  
...  
Keyword(s):  
Conformational Preferences

Conformational preferences of peptide-peptoid hybrid oligomers

Biopolymers ◽  
2014 ◽  
Vol 102 (5) ◽  
pp. 369-378 ◽  
Author(s):  
Glenn L. Butterfoss ◽  
Kevin Drew ◽  
P. Douglas Renfrew ◽  
Kent Kirshenbaum ◽  
Richard Bonneau
Keyword(s):  
Conformational Preferences

scholarly journals Functionalised Terpyridines and Their Metal Complexes—Solid-State Interactions

Chemistry ◽  
2021 ◽  
Vol 3 (1) ◽  
pp. 199-227
Author(s):  
Young Hoon Lee ◽  
Jee Young Kim ◽  
Sotaro Kusumoto ◽  
Hitomi Ohmagari ◽  
Miki Hasegawa ◽  
...  
Keyword(s):  
Solid State ◽  
Metal Complexes ◽  
Crystal Structures ◽  
Weak Interactions ◽  
Dispersion Interactions ◽  
Derivatives Of

Analysis of the weak interactions within the crystal structures of 33 complexes of various 4′-aromatic derivatives of 2,2′:6′,2″-terpyridine (tpy) shows that interactions that exceed dispersion are dominated, as expected, by cation⋯anion contacts but are associated with both ligand–ligand and ligand–solvent contacts, sometimes multicentred, in generally complicated arrays, probably largely determined by dispersion interactions between stacked aromatic units. With V(V) as the coordinating cation, there is evidence that the polarisation of the ligand results in an interaction exceeding dispersion at a carbon bound to nitrogen with oxygen or fluorine, an interaction unseen in the structures of M(II) (M = Fe, Co, Ni, Cu, Zn, Ru and Cd) complexes, except when 1,2,3-trimethoxyphenyl substituents are present in the 4′-tpy.

scholarly journals Accurate prediction of terahertz spectra of molecular crystals of fentanyl and its analogs

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Chun-Hung Wang ◽  
Anthony C. Terracciano ◽  
Artёm E. Masunov ◽  
Mengyu Xu ◽  
Subith S. Vasu
Keyword(s):  
Molecular Structure ◽  
Crystal Packing ◽  
Molecular Crystals ◽  
Normal Modes ◽  
Rapid Identification ◽  
Medical Attention ◽  
Dispersion Interactions ◽  
Pain Reliever ◽  
Fentanyl Analogs ◽  
High Bioavailability

AbstractFentanyl is a potent synthetic opioid pain reliever with a high bioavailability that can be used as prescription anesthetic. Rapid identification via non-contact methods of both known and emerging opioid substances in the fentanyl family help identify the substances and enable rapid medical attention. We apply PBEh-3c method to identify vibrational normal modes from 0.01 to 3 THz in solid fentanyl and its selected analogs. The molecular structure of each fentanyl analog and unique arrangement of H-bonds and dispersion interactions significantly change crystal packing and is subsequently reflected in the THz spectrum. Further, the study of THz spectra of a series of stereoisomers shows that small changes in molecular structure results in distinct crystal packing and significantly alters THz spectra as well. We discuss spectral features of synthetic opioids with higher potency than conventional fentanyl such as ohmefentanyl and sufentanil and discover the pattern of THz spectra of fentanyl analogs.

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