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Article: Approaches to primary tert-alkyl amines as building blocks

Tzitzoglaki, Christina / Drakopoulos, Antonios / Kolocouris, Antonios / Konstantinidi, Athina / Stampolaki, Marianna / Stylianakis, Ioannis

Tetrahedron. 2019 June 11,

2019

Abstract: Primary tert-alkyl amines include analogues of amantadine, a fragment commonly linked to pharmacophoric groups to enhance biological activity. The preparation of primary tert-alkyl amines is considered to be a difficult problem. Four synthetic procedures, ...

Abstract	Primary tert-alkyl amines include analogues of amantadine, a fragment commonly linked to pharmacophoric groups to enhance biological activity. The preparation of primary tert-alkyl amines is considered to be a difficult problem. Four synthetic procedures, some of which have been previously reported for the synthesis of amines with primary (RCH2NH2) or secondary (RR'CHNH2) alkyl and/or aryl groups, were tested for the synthesis of primary tert-alkyl amines (RR′R′′CNH2) in aliphatic series including adamantane adducts. These procedures included the formation and reduction of tert-alkyl azides, the Ritter reaction in standard and modified conditions, the addition of organometallic reagents to N-tert-butyl sulfinyl ketimines and one-pot reactions between nitriles and organometallic reagents in the presence of a Lewis acid, Τi(iPrO)4 or CeCl3. These synthetic routes are unexplored for primary tert-alkyl amines. Studies on the synthetic routes for primary tert-alkyl amines are currently lacking. The reaction conditions and substrate limitations were studied for each procedure, with the first procedure being the most general and applicable also for compounds bearing bulky adducts.
Keywords	amines ; azides ; bioactive properties ; chemical reactions ; ketimines ; Lewis acids ; moieties ; nitriles ; organic chemistry
Language	English
Dates of publication	2019-0611
Publishing place	Elsevier Ltd
Document type	Article
Note	Pre-press version
ZDB-ID	204285-x
ISSN	1464-5416 ; 0040-4020 ; 0563-2064
ISSN (online)	1464-5416
ISSN	0040-4020 ; 0563-2064
DOI	10.1016/j.tet.2019.06.016
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: A Study of the Activity of Adamantyl Amines against Mutant Influenza A M2 Channels Identified a Polycyclic Cage Amine Triple Blocker, Explored by Molecular Dynamics Simulations and Solid-State NMR.

Stampolaki, Μarianna / Hoffmann, Anja / Tekwani, Kumar / Georgiou, Kyriakos / Tzitzoglaki, Christina / Ma, Chunlong / Becker, Stefan / Schmerer, Patrick / Döring, Kristin / Stylianakis, Ioannis / Turcu, Andreea L / Wang, Jun / Vázquez, Santiago / Andreas, Loren B / Schmidtke, Michaela / Kolocouris, Antonios

ChemMedChem

2023 Volume 18, Issue 16, Page(s) e202300182

Abstract: We compared the anti-influenza potencies of 57 adamantyl amines and analogs against influenza A virus with serine-31 M2 proton channel, usually termed as WT M2 channel, which is amantadine sensitive. We also tested a subset of these compounds against ... ...

Abstract	We compared the anti-influenza potencies of 57 adamantyl amines and analogs against influenza A virus with serine-31 M2 proton channel, usually termed as WT M2 channel, which is amantadine sensitive. We also tested a subset of these compounds against viruses with the amantadine-resistant L26F, V27A, A30T, G34E M2 mutant channels. Four compounds inhibited WT M2 virus in vitro with mid-nanomolar potency, with 27 compounds showing sub-micromolar to low micromolar potency. Several compounds inhibited L26F M2 virus in vitro with sub-micromolar to low micromolar potency, but only three compounds blocked L26F M2-mediated proton current as determined by electrophysiology (EP). One compound was found to be a triple blocker of WT, L26F, V27A M2 channels by EP assays, but did not inhibit V27A M2 virus in vitro, and one compound inhibited WT, L26F, V27A M2 in vitro without blocking V27A M2 channel. One compound blocked only L26F M2 channel by EP, but did not inhibit virus replication. The triple blocker compound is as long as rimantadine, but could bind and block V27A M2 channel due to its larger girth as revealed by molecular dynamics simulations, while MAS NMR informed on the interaction of the compound with M2(18-60) WT or L26F or V27A.
MeSH term(s)	Humans ; Molecular Dynamics Simulation ; Antiviral Agents/chemistry ; Amines/pharmacology ; Protons ; Mutation ; Influenza, Human/drug therapy ; Amantadine/pharmacology ; Amantadine/therapeutic use ; Viral Matrix Proteins/chemistry ; Drug Resistance, Viral
Chemical Substances	Antiviral Agents ; Amines ; Protons ; Amantadine (BF4C9Z1J53) ; Viral Matrix Proteins
Language	English
Publishing date	2023-07-25
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2218496-X
ISSN	1860-7187 ; 1860-7179
ISSN (online)	1860-7187
ISSN	1860-7179
DOI	10.1002/cmdc.202300182
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Amantadine variant – aryl conjugates that inhibit multiple M2 mutant – amantadine resistant influenza a viruses

Christina Tzitzoglaki / Anja Hoffmann / Andreea L. Turcu / Patrick Schmerer / Chunlong Ma / George Laros / Christos Liolios / Brea José / Jun Wang / Santiago Vázquez / Michaela Schmidtke / Antonios Kolocouris

European Journal of Medicinal Chemistry Reports, Vol 6, Iss , Pp 100083- (2022)

2022

Abstract: Influenza A viruses can cause a serious future threat due to frequent mutations. Amantadine and rimantadine drugs inhibit influenza A M2 wild-type (WT; bearing in the protein M2 proton channel serine at position-31) viruses by binding and blocking M2 WT ... ...

Abstract	Influenza A viruses can cause a serious future threat due to frequent mutations. Amantadine and rimantadine drugs inhibit influenza A M2 wild-type (WT; bearing in the protein M2 proton channel serine at position-31) viruses by binding and blocking M2 WT channel-mediated proton current. The resistant to these drugs influenza A viruses bearing the S31N mutant in the M2 proton channel can be inhibited by amantadine – aryl conjugates, in which amantadine and an aryl group are linked through a methylene, which block M2 S31N channel-mediated proton current. However, the M2 amantadine/rimantadine resistant viruses bearing one of the four mutations L26F, V27A, A30T, G34E in residues that line the M2 channel pore pose an additional concern for public health.Here, we designed 33 compounds based on the structure of three previously published and potent amantadine-aryl conjugates against M2 S31N virus, by replacing amantadine with 16 amantadine variants. The compounds were tested against M2 WT and the five M2 amantadine resistant viruses aiming at identifying inhibitors against multiple M2 mutant – amantadine resistant viruses.We identified 16 compounds that inhibited in vitro two influenza A viruses with M2 WT or L26F channels. Additionally, compounds 21 or 32 or 33, which are conjugates of the rimantadine variant with CMe2 (instead of CHMe in rimantadine) or the diamantylamine or the 4-(1-adamantyl)benzenamine with the 2-hydroxy-4-methoxyphenyl aryl group, were in vitro inhibitors against three influenza A viruses with M2 WT or L26F or S31N, while compound 21 inhibited also in vitro the M2 G34E virus and compound 32 inhibited also in vitro the M2 A30T virus. Also, using electrophysiology, we showed that compound 21 was an efficient blocker of the M2 WT and M2 L26F channels, compound 32 blocked efficiently the M2 WT channel and compound 33 blocked the M2 WT, L26F and V27A channels. The drug metabolism and pharmacokinetics studies showed that these compounds need further optimization.
Keywords	Amantadine - aryl conjugate ; In vitro antiviral activity ; CPE ; Electrophysiology ; Influenza A M2 protein ; A30T ; Pharmacy and materia medica ; RS1-441 ; Other systems of medicine ; RZ201-999
Subject code	572 ; 500
Language	English
Publishing date	2022-12-01T00:00:00Z
Publisher	Elsevier
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Chemical Probes for Blocking of Influenza A M2 Wild-type and S31N Channels.

Tzitzoglaki, Christina / McGuire, Kelly / Lagarias, Panagiotis / Konstantinidi, Athina / Hoffmann, Anja / Fokina, Natalie A / Ma, Chulong / Papanastasiou, Ioannis P / Schreiner, Peter R / Vázquez, Santiago / Schmidtke, Michaela / Wang, Jun / Busath, David D / Kolocouris, Antonios

ACS chemical biology

2020 Volume 15, Issue 9, Page(s) 2331–2337

Abstract: We report on using the synthetic aminoadamantane- ... ...

Abstract	We report on using the synthetic aminoadamantane-CH
MeSH term(s)	Adamantane/analogs & derivatives ; Adamantane/chemistry ; Adamantane/metabolism ; Adamantane/pharmacology ; Betacoronavirus/drug effects ; Binding Sites ; COVID-19 ; Cells, Cultured ; Chloroquine/pharmacology ; Coronavirus Infections/drug therapy ; Coronavirus Infections/prevention & control ; Genetic Variation ; Humans ; Influenza A virus/chemistry ; Influenza A virus/drug effects ; Influenza A virus/genetics ; Influenza, Human/drug therapy ; Influenza, Human/prevention & control ; Ion Channels/antagonists & inhibitors ; Kinetics ; Molecular Probes/chemistry ; Molecular Probes/metabolism ; Pandemics/prevention & control ; Pneumonia, Viral/drug therapy ; Pneumonia, Viral/prevention & control ; Protein Binding ; SARS-CoV-2 ; Structure-Activity Relationship ; Viral Matrix Proteins/antagonists & inhibitors ; Virus Replication/drug effects
Chemical Substances	Ion Channels ; M2 protein, Influenza A virus ; Molecular Probes ; Viral Matrix Proteins ; Chloroquine (886U3H6UFF) ; Adamantane (PJY633525U)
Keywords	covid19
Language	English
Publishing date	2020-08-27
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1554-8937
ISSN (online)	1554-8937
DOI	10.1021/acschembio.0c00553
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Affinity of Rimantadine Enantiomers against Influenza A/M2 Protein Revisited.

Drakopoulos, Antonios / Tzitzoglaki, Christina / Ma, Chulong / Freudenberger, Kathrin / Hoffmann, Anja / Hu, Yanmei / Gauglitz, Günter / Schmidtke, Michaela / Wang, Jun / Kolocouris, Antonios

ACS medicinal chemistry letters

2017 Volume 8, Issue 2, Page(s) 145–150

Abstract: Recent findings from solid state NMR (ssNMR) studies suggested that the ( ...

Abstract	Recent findings from solid state NMR (ssNMR) studies suggested that the (
Language	English
Publishing date	2017-01-27
Publishing country	United States
Document type	Journal Article
ISSN	1948-5875
ISSN	1948-5875
DOI	10.1021/acsmedchemlett.6b00311
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Unraveling the Binding, Proton Blockage, and Inhibition of Influenza M2 WT and S31N by Rimantadine Variants.

Drakopoulos, Antonios / Tzitzoglaki, Christina / McGuire, Kelly / Hoffmann, Anja / Konstantinidi, Athina / Kolokouris, Dimitrios / Ma, Chunlong / Freudenberger, Kathrin / Hutterer, Johanna / Gauglitz, Günter / Wang, Jun / Schmidtke, Michaela / Busath, David D / Kolocouris, Antonios

ACS medicinal chemistry letters

2018 Volume 9, Issue 3, Page(s) 198–203

Abstract: Recently, the binding kinetics of a ligand-target interaction, such as the residence time of a small molecule on its protein target, are seen as increasingly important for drug efficacy. Here, we investigate these concepts to explain binding and proton ... ...

Abstract	Recently, the binding kinetics of a ligand-target interaction, such as the residence time of a small molecule on its protein target, are seen as increasingly important for drug efficacy. Here, we investigate these concepts to explain binding and proton blockage of rimantadine variants bearing progressively larger alkyl groups to influenza A virus M2 wild type (WT) and M2 S31N protein proton channel. We showed that resistance of M2 S31N to rimantadine analogues compared to M2 WT resulted from their higher
Language	English
Publishing date	2018-01-29
Publishing country	United States
Document type	Journal Article
ISSN	1948-5875
ISSN	1948-5875
DOI	10.1021/acsmedchemlett.7b00458
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Chemical Probes for Blocking of Influenza A M2 Wild-type and S31N Channels

ACS Chem Biol

Abstract: We report on using the synthetic aminoadamantane-CH2-aryl derivatives 1-6 as sensitive probes for blocking M2 S31N and influenza A virus (IAV) M2 wild-type (WT) channels as well as virus replication in cell culture. The binding kinetics measured using ... ...

Abstract	We report on using the synthetic aminoadamantane-CH2-aryl derivatives 1-6 as sensitive probes for blocking M2 S31N and influenza A virus (IAV) M2 wild-type (WT) channels as well as virus replication in cell culture. The binding kinetics measured using electrophysiology (EP) for M2 S31N channel are very dependent on the length between the adamantane moiety and the first ring of the aryl headgroup realized in 2 and 3 and the girth and length of the adamantane adduct realized in 4 and 5. Study of 1-6 shows that, according to molecular dynamics (MD) simulations and molecular mechanics Poisson-Boltzmann surface area (MM/PBSA) calculations, all bind in the M2 S31N channel with the adamantyl group positioned between V27 and G34 and the aryl group projecting out of the channel with the phenyl (or isoxazole in 6) embedded in the V27 cluster. In this outward binding configuration, an elongation of the ligand by only one methylene in rimantadine 2 or using diamantane or triamantane instead of adamantane in 4 and 5, respectively, causes incomplete entry and facilitates exit, abolishing effective block compared to the amantadine derivatives 1 and 6. In the active M2 S31N blockers 1 and 6, the phenyl and isoxazolyl head groups achieve a deeper binding position and high kon/low koff and high kon/high koff rate constants, compared to inactive 2-5, which have much lower kon and higher koff. Compounds 1-5 block the M2 WT channel by binding in the longer area from V27-H37, in the inward orientation, with high kon and low koff rate constants. Infection of cell cultures by influenza virus containing M2 WT or M2 S31N is inhibited by 1-5 or 1-4 and 6, respectively. While 1 and 6 block infection through the M2 block mechanism in the S31N variant, 2-4 may block M2 S31N virus replication in cell culture through the lysosomotropic effect, just as chloroquine is thought to inhibit SARS-CoV-2 infection.
Keywords	covid19
Publisher	WHO
Document type	Article
Note	WHO #Covidence: #714371
Database	COVID19

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Article ; Online: Binding and Proton Blockage by Amantadine Variants of the Influenza M2

Tzitzoglaki, Christina / Wright, Anna / Freudenberger, Kathrin / Hoffmann, Anja / Tietjen, Ian / Stylianakis, Ioannis / Kolarov, Felix / Fedida, David / Schmidtke, Michaela / Gauglitz, Günter / Cross, Timothy A / Kolocouris, Antonios

Journal of medicinal chemistry

2017 Volume 60, Issue 5, Page(s) 1716–1733

Abstract: While aminoadamantanes are well-established inhibitors of the influenza A M2 proton channel, the mechanisms by which they are rendered ineffective against ... ...

Abstract	While aminoadamantanes are well-established inhibitors of the influenza A M2 proton channel, the mechanisms by which they are rendered ineffective against M2
MeSH term(s)	Amantadine/pharmacology ; Antiviral Agents/pharmacology ; Influenza A virus/drug effects ; Ligands ; Protons ; Spectrum Analysis ; Viral Matrix Proteins/antagonists & inhibitors ; Viral Matrix Proteins/metabolism
Chemical Substances	Antiviral Agents ; Ligands ; M2 protein, Influenza A virus ; Protons ; Viral Matrix Proteins ; Amantadine (BF4C9Z1J53)
Language	English
Publishing date	2017-02-15
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	218133-2
ISSN	1520-4804 ; 0022-2623
ISSN (online)	1520-4804
ISSN	0022-2623
DOI	10.1021/acs.jmedchem.6b01115
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Article ; Online: Aminoadamantanes with persistent in vitro efficacy against H1N1 (2009) influenza A.

Kolocouris, Antonios / Tzitzoglaki, Christina / Johnson, F Brent / Zell, Roland / Wright, Anna K / Cross, Timothy A / Tietjen, Ian / Fedida, David / Busath, David D

Journal of medicinal chemistry

2014 Volume 57, Issue 11, Page(s) 4629–4639

Abstract: A series of 2-adamantanamines with alkyl adducts of various lengths were examined for efficacy against strains of influenza A including those having an S31N mutation in M2 proton channel that confer resistance to amantadine and rimantadine. The addition ... ...

Abstract	A series of 2-adamantanamines with alkyl adducts of various lengths were examined for efficacy against strains of influenza A including those having an S31N mutation in M2 proton channel that confer resistance to amantadine and rimantadine. The addition of as little as one CH2 group to the methyl adduct of the amantadine/rimantadine analogue, 2-methyl-2-aminoadamantane, led to activity in vitro against two M2 S31N viruses A/Calif/07/2009 (H1N1) and A/PR/8/34 (H1N1) but not to a third A/WS/33 (H1N1). Solid state NMR of the transmembrane domain (TMD) with a site mutation corresponding to S31N shows evidence of drug binding. But electrophysiology using the full length S31N M2 protein in HEK cells showed no blockade. A wild type strain, A/Hong Kong/1/68 (H3N2) developed resistance to representative drugs within one passage with mutations in M2 TMD, but A/Calif/07/2009 S31N was slow (>8 passages) to develop resistance in vitro, and the resistant virus had no mutations in M2 TMD. The results indicate that 2-alkyl-2-aminoadamantane derivatives with sufficient adducts can persistently block p2009 influenza A in vitro through an alternative mechanism. The observations of an HA1 mutation, N160D, near the sialic acid binding site in both 6-resistant A/Calif/07/2009(H1N1) and the broadly resistant A/WS/33(H1N1) and of an HA1 mutation, I325S, in the 6-resistant virus at a cell-culture stable site suggest that the drugs tested here may block infection by direct binding near these critical sites for virus entry to the host cell.
MeSH term(s)	Adamantane/analogs & derivatives ; Adamantane/chemical synthesis ; Adamantane/pharmacology ; Amantadine/pharmacology ; Animals ; Antiviral Agents/chemical synthesis ; Antiviral Agents/pharmacology ; Dogs ; Drug Resistance, Multiple, Viral ; HEK293 Cells ; Humans ; Influenza A Virus, H1N1 Subtype/drug effects ; Influenza A Virus, H1N1 Subtype/genetics ; Ion Channels/genetics ; Madin Darby Canine Kidney Cells ; Mutation ; Rimantadine/pharmacology ; Viral Matrix Proteins/genetics
Chemical Substances	Antiviral Agents ; Ion Channels ; M2 protein, Influenza A virus ; Viral Matrix Proteins ; Rimantadine (0T2EF4JQTU) ; Amantadine (BF4C9Z1J53) ; Adamantane (PJY633525U)
Language	English
Publishing date	2014-05-15
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	218133-2
ISSN	1520-4804 ; 0022-2623
ISSN (online)	1520-4804
ISSN	0022-2623
DOI	10.1021/jm500598u
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Article ; Online: Alchemical Free Energy Calculations and Isothermal Titration Calorimetry Measurements of Aminoadamantanes Bound to the Closed State of Influenza A/M2TM.

Ioannidis, Harris / Drakopoulos, Antonios / Tzitzoglaki, Christina / Homeyer, Nadine / Kolarov, Felix / Gkeka, Paraskevi / Freudenberger, Kathrin / Liolios, Christos / Gauglitz, Günter / Cournia, Zoe / Gohlke, Holger / Kolocouris, Antonios

Journal of chemical information and modeling

2016 Volume 56, Issue 5, Page(s) 862–876

Abstract: Adamantane derivatives, such as amantadine and rimantadine, have been reported to block the transmembrane domain (TM) of the M2 protein of influenza A virus (A/M2) but their clinical use has been discontinued due to evolved resistance in humans. Although ...

Abstract	Adamantane derivatives, such as amantadine and rimantadine, have been reported to block the transmembrane domain (TM) of the M2 protein of influenza A virus (A/M2) but their clinical use has been discontinued due to evolved resistance in humans. Although experiments and simulations have provided adequate information about the binding interaction of amantadine or rimantadine to the M2 protein, methods for predicting binding affinities of whole series of M2 inhibitors have so far been scarcely applied. Such methods could assist in the development of novel potent inhibitors that overcome A/M2 resistance. Here we show that alchemical free energy calculations of ligand binding using the Bennett acceptance ratio (BAR) method are valuable for determining the relative binding potency of A/M2 inhibitors of the aminoadamantane type covering a binding affinity range of only ∼2 kcal mol(-1). Their binding affinities measured by isothermal titration calorimetry (ITC) against the A/M2TM tetramer from the Udorn strain in its closed form at pH 8 were used as experimental probes. The binding constants of rimantadine enantiomers against M2TMUdorn were measured for the first time and found to be equal. Two series of alchemical free energy calculations were performed using 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) and 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) lipids to mimic the membrane environment. A fair correlation was found for DPPC that was significantly improved using DMPC, which resembles more closely the DPC lipids used in the ITC experiments. This demonstrates that binding free energy calculations by the BAR approach can be used to predict relative binding affinities of aminoadamantane derivatives toward M2TM with good accuracy.
MeSH term(s)	Adamantane/chemistry ; Adamantane/metabolism ; Amino Acid Sequence ; Calorimetry ; Cell Membrane/metabolism ; Entropy ; Humans ; Molecular Dynamics Simulation ; Protein Binding ; Protein Domains ; Protons ; Stereoisomerism ; Temperature ; Viral Matrix Proteins/chemistry ; Viral Matrix Proteins/metabolism
Chemical Substances	M2 protein, Influenza A virus ; Protons ; Viral Matrix Proteins ; Adamantane (PJY633525U)
Language	English
Publishing date	2016-05-23
Publishing country	United States
Document type	Journal Article
ZDB-ID	190019-5
ISSN	1549-960X ; 0095-2338
ISSN (online)	1549-960X
ISSN	0095-2338
DOI	10.1021/acs.jcim.6b00079
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