Quadruple hydrogen bonds and thermo-triggered hydrophobic interactions generate dynamic hydrogels to modulate transplanted cell retention

2019 ◽  
Vol 7 (4) ◽  
pp. 1286-1298 ◽  
Author(s):  
Sa Liu ◽  
Dawei Qi ◽  
Yunhua Chen ◽  
Lijing Teng ◽  
Yongguang Jia ◽  
...  
Keyword(s):  
Hydrogen Bonds ◽  
Hydrophobic Interactions ◽  
Cell Retention

Supramolecular dynamic hydrogels with quadruple hydrogen bonds and thermo-triggered hydrophobic interactions demonstrate a promising capability of modulating transplanted cell retention.

scholarly journals The Subtleties of Dissolution and Regeneration of Cellulose: Breaking and Making Hydrogen Bonds

BioResources ◽  
2015 ◽  
Vol 10 (3) ◽  
pp. 3811-3814 ◽  
Author(s):  
Björn Lindman ◽  
Bruno Medronho
Keyword(s):  
Hydrogen Bonding ◽  
Hydrogen Bonds ◽  
Hydrophobic Interactions ◽  
Cellulose Dissolution ◽  
Solution Behavior ◽  
Current Discussion ◽  
Scientific Controversies ◽  
A Current

Cellulose dissolution and regeneration are old topics that have recently gained renewed attention. This is reflected in both applications – earlier and novel – and in scientific controversies. There is a current discussion in the literature on the balance between hydrogen bonding and hydrophobic interactions in controlling the solution behavior of cellulose. Some of the key ideas are recalled.

Models for the binding channel of wild type and mutant transthyretin with glabridin

RSC Advances ◽  
2016 ◽  
Vol 6 (99) ◽  
pp. 96816-96823 ◽  
Author(s):  
Liyun Zou ◽  
Jingxuan Zhu ◽  
Yang Dong ◽  
Weiwei Han ◽  
Yingjie Guo ◽  
...  
Keyword(s):  
Hydrogen Bonds ◽  
Hydrophobic Interactions ◽  
Wild Type ◽  
Binding Interface

Our results indicate that additional high-occupancy hydrogen bonds were observed at the binding interface between the two dimers in V30A TTR, while stabilisation hydrophobic interactions between residues in the mutant AB loop decreased.

scholarly journals Can two wrongs make a right? F508del-CFTR ion channel rescue by second-site mutations in its transmembrane domains

2021 ◽  
Author(s):  
Stella Prins ◽  
Valentina Corradi ◽  
David N. Sheppard ◽  
D. Peter Tieleman ◽  
Paola Vergani
Keyword(s):  
Cystic Fibrosis ◽  
Hydrogen Bonds ◽  
Ion Channel ◽  
Hydrophobic Interactions ◽  
Anion Channel ◽  
Transmembrane Helices ◽  
Aromatic Rings ◽  
Intracellular Loop ◽  
Dynamic Interface ◽  
Dynamics Simulations

AbstractDeletion of phenylalanine 508 (F508del), in the cystic fibrosis transmembrane conductance regulator (CFTR) anion channel, is the most common cause of cystic fibrosis (CF). F508 is located on nucleotide-binding domain 1 (NBD1) in contact with cytosolic extensions of transmembrane helices, in particular intracellular loop 4 (ICL4). We carried out a mutagenesis scan of ICL4 by introducing five or six second-site mutations at eleven positions in cis with F508del, and quantifying changes in membrane proximity and ion-channel function of CFTR. The scan strongly validated the effectiveness of R1070W at rescuing F508del defects. Molecular dynamics simulations highlighted two features characterizing the ICL4/NBD1 interface of F508del/R1070W-CFTR: flexibility, with frequent transient formation of interdomain hydrogen bonds, and loosely stacked aromatic sidechains, (F1068, R1070W, and F1074, mimicking F1068, F508 and F1074 in wild-type CFTR). F508del-CFTR had a distorted aromatic stack, with F1068 displaced towards space vacated by F508. In F508del/R1070F-CFTR, which largely retained F508del defects, R1070F could not form hydrogen bonds, and the interface was less flexible. Other ICL4 second-site mutations which partially rescued F508del-CFTR are F1068M and F1074M. Methionine side chains allow hydrophobic interactions without the steric rigidity of aromatic rings, possibly conferring flexibility to accommodate the absence of F508 and retain a dynamic interface. Finally, two mutations identified in a yeast scan (A141S and R1097T, on adjacent transmembrane helices linked to ICL1 and ICL4) also partially rescued F508del-CFTR function. These studies highlight the importance of hydrophobic interactions and conformational flexibility at the ICL4/NBD1 interface, advancing understanding of the structural underpinning of F508del dysfunction.

scholarly journals Crystal structure ofmeso-3,3′-(1,4-phenylene)bis(2-phenyl-2,3,5,6-tetrahydro-4H-1,3-thiazin-4-one)

2018 ◽  
Vol 74 (10) ◽  
pp. 1497-1499
Author(s):  
Hemant P. Yennawar ◽  
Quentin J. Moyer ◽  
Lee J. Silverberg
Keyword(s):  
Crystal Structure ◽  
Carbon Atom ◽  
Hydrogen Bonds ◽  
Title Compound ◽  
Phenyl Ring ◽  
Hydrophobic Interactions ◽  
The Other ◽  
Asymmetric Unit ◽  
Phenyl Rings ◽  
Thiazine Ring

The crystal structure of the title compound –meso-C26H24N2O2S2with two stereocenters – has half the molecule in the asymmetric unit with the other half generated by a crystallographic center of inversion. The thiazine ring is in a conformation that is between half-chair and envelope [θ = 52.51 (17)°]. The phenyl ring on the 2-carbon atom of the thiazine ring is pseudo-axial. The central phenyl ring of the molecule is close to orthogonal to the phenyl rings on either side with an angle of 76.85 (11)° between those planes. In the crystal, pairwise, weak C—H...O hydrogen bonds between the central phenyl ring and the oxygen atoms of neighboring molecules result in continuous strips propagating along thea-axis direction. Hydrophobic interactions of the C—H...π type are also observed.

The influence of a type III antifreeze protein and its mutants on methane hydrate adsorption–inhibition: a molecular dynamics simulation study

2019 ◽  
Vol 21 (39) ◽  
pp. 21836-21846 ◽  
Author(s):  
Mitra Maddah ◽  
Mina Maddah ◽  
Kiana Peyvandi
Keyword(s):  
Molecular Dynamics ◽  
Amino Acids ◽  
Molecular Dynamics Simulation ◽  
Hydrogen Bonds ◽  
Simulation Study ◽  
Methane Hydrate ◽  
Hydrophobic Interactions ◽  
Dynamics Simulation ◽  
Antifreeze Activity ◽  
Adsorption Inhibition

Antifreeze proteins inhibit hydrate growth by hydrophobic interactions in cooperation with hydrogen bonds. Mutation of three polar amino acids (Asn14, Thr18, and Gln44) elucidates the molecular mechanism of AFP III antifreeze activity.

Di(phenylpropylamino)gossypol: a derivative of the dimeric natural product gossypol

2013 ◽  
Vol 69 (4) ◽  
pp. 439-443 ◽  
Author(s):  
Carlos A. Zelaya ◽  
Edwin D. Stevens ◽  
Michael K. Dowd
Keyword(s):  
Hydrogen Bonds ◽  
Natural Product ◽  
Room Temperature ◽  
Hydrophobic Interactions ◽  
Naphthalene Ring ◽  
Intermolecular Hydrogen Bonds ◽  
Schiff Base Derivatives ◽  
Pendent Groups ◽  
Centrosymmetric Dimers ◽  
Additional Hydrogen

Di(phenylpropylamino)gossypol [systematic name: 2,2′-bis{1,6-dihydroxy-5-isopropyl-8-[(3-phenylpropylamino)methylidene]naphthalen-7-one}, C48H52N2O6, was formed by reaction of the dimeric natural product gossypol with 3-phenylpropylamine. The structure of this compound has its two naphthalene ring systems oriented approximately perpendicular to each other, and the two pendant phenylpropyl groups have different conformations. One of these side groups is considerably disordered at room temperature but less so at 120 K. The enantiomeric molecules form centrosymmetric dimers that are supported by intermolecular hydrogen bonds and by hydrophobic interactions between a pair of naphthalene rings. Two additional hydrogen bonds tie the dimer pairs into layers. Unlike gossypol and many gossypol Schiff base derivatives, the title compound crystallizes without the inclusion of solvent, which appears to occur because of the size and flexibility of its phenylpropyl pendent groups.

scholarly journals Crystal structure of the Y52F/Y73F double mutant of phospholipase A2: Increased hydrophobic interactions of the phenyl groups compensate for the disrupted hydrogen bonds of the tyrosines

1992 ◽  
Vol 1 (12) ◽  
pp. 1585-1594 ◽  
Author(s):  
Chandra Sekharudu ◽  
Boopathy Ramakrishnan ◽  
Baohua Huang ◽  
Ru-Tai Jiang ◽  
Cynthia M. Dupureur ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Hydrogen Bonds ◽  
Phospholipase A2 ◽  
Double Mutant ◽  
Hydrophobic Interactions
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